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Conserved domains on  [gi|8923559|ref|NP_060367|]
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3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase II( domain architecture ID 11496422)

beta-ketoacyl-[acyl-carrier-protein] synthase II catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP, part of the dissociated (or type II) fatty acid biosynthesis system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 42-455 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


:

Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 588.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 8923559    441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 42-455 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 588.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 8923559    441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 42-456 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 587.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  122 AIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:cd00834  75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:cd00834 234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:cd00834 314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                       410
                ....*....|....*.
gi 8923559  441 LTNSFGFGGTNATLCI 456
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
42-454 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 585.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKD------FNPDDYMSRKEARRMDRFIQY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK07314  76 GIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAET 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:PRK07314 315 QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---YA 391

                        410
                 ....*....|....
gi 8923559   441 LTNSFGFGGTNATL 454
Cdd:PRK07314 392 LSNSFGFGGTNASL 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 42-456 0e+00

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 576.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:COG0304  75 ALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:COG0304 314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390

                       410
                ....*....|....*.
gi 8923559  441 LTNSFGFGGTNATLCI 456
Cdd:COG0304 391 LSNSFGFGGHNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 42-291 5.45e-56

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 186.30  E-value: 5.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGE-----EYKSIPCSVA--AYVPRG--SDEGQFNEQNF-VSKSD 111
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGglDDIFDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    112 IKSMSSPTIMAIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMiplEVVSETALNFQTKGYNKVSPFFVPKIlVNMAAGQ 191
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSL-DGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNsDPklaCRPFHPKR 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231

                         250       260
                  ....*....|....*....|
gi 8923559    272 DGFVMGEGAAVLVLEEYEHA 291
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 204-452 1.77e-27

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 111.27  E-value: 1.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     204 AVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSdpklACRPFHPKRDGFVMGEGAAVL 283
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDG----RCKTFDASADGYVRGEGVGVV 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     284 VLEEYEHAVQRRARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaalkdagvQpeeisyinahatstplgdaaenk 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA----------------Q----------------------- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     362 aikhlfkdhayaLAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTE 435
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274

                          250
                   ....*....|....*....
gi 8923559     436 --KRFIGLtNSFGFGGTNA 452
Cdd:smart00825 275 grPRRAGV-SSFGFGGTNA 292
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 42-455 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 588.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 8923559    441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 42-456 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 587.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  122 AIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:cd00834  75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:cd00834 234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:cd00834 314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                       410
                ....*....|....*.
gi 8923559  441 LTNSFGFGGTNATLCI 456
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
42-454 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 585.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKD------FNPDDYMSRKEARRMDRFIQY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK07314  76 GIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAET 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:PRK07314 315 QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---YA 391

                        410
                 ....*....|....
gi 8923559   441 LTNSFGFGGTNATL 454
Cdd:PRK07314 392 LSNSFGFGGTNASL 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 42-456 0e+00

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 576.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:COG0304  75 ALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:COG0304 314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390

                       410
                ....*....|....*.
gi 8923559  441 LTNSFGFGGTNATLCI 456
Cdd:COG0304 391 LSNSFGFGGHNASLVF 406
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 41-454 0e+00

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 532.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    41 HRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYK--------------SIPCSVAAYVPRGSDEGQFNEQNF 106
Cdd:PLN02836   5 TRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKmksedeetqlytldQLPSRVAALVPRGTGPGDFDEELW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   107 VSKsdiKSMSSPTIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVN 186
Cdd:PLN02836  85 LNS---RSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   187 MAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLAC 264
Cdd:PLN02836 162 MAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEAS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   265 RPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISY 344
Cdd:PLN02836 242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDY 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   345 INAHATSTPLGDAAENKAIKHLFKDHAY--ALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDL 422
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDD 401

                        410       420       430
                 ....*....|....*....|....*....|..
gi 8923559   423 NYVPLKAQewKTEKRFIGLTNSFGFGGTNATL 454
Cdd:PLN02836 402 GFVPLTAS--KAMLIRAALSNSFGFGGTNASL 431
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
41-454 3.41e-176

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 499.91  E-value: 3.41e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    41 HRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSD--EGQFNEQNFVSKSDIKSMSSP 118
Cdd:PRK06333   3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDLAEdaEAGFDPDRYLDPKDQRKMDRF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKL 198
Cdd:PRK06333  83 ILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   199 KGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLACRPFHPKRDGFVM 276
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGFVM 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   277 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 356
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   357 AAENKAIKHLFKdHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQEWKTE 435
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401

                        410
                 ....*....|....*....
gi 8923559   436 krfIGLTNSFGFGGTNATL 454
Cdd:PRK06333 402 ---YALSNGFGFGGVNASI 417
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 51-454 5.87e-170

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 484.20  E-value: 5.87e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    51 LVTPLGVGTHLVWDRLIGGESGIVSLVGEEYK----------------SIPCSVAAYVPrgsdegqfNEQNFVSKSDIKS 114
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEVD--------QSEFDPSDFAPTK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   115 MSSPTI-MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVS 193
Cdd:PTZ00050  73 RESRAThFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   194 IRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLACRPFHPKR 271
Cdd:PTZ00050 153 IKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKDR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   272 DGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAG-VQPEEISYINAHAT 350
Cdd:PTZ00050 233 AGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHAT 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   351 STPLGDAAENKAIKHLFKDH-AYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKA 429
Cdd:PTZ00050 313 STPIGDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKT 392

                        410       420
                 ....*....|....*....|....*
gi 8923559   430 QEWKTEKRfIGLTNSFGFGGTNATL 454
Cdd:PTZ00050 393 AHPLQSID-AVLSTSFGFGGVNTAL 416
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
42-454 7.92e-127

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 374.34  E-value: 7.92e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK08722   4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMDLFIQY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   122 AIGAAELAMKDSGWHpQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK08722  78 GIAAGIQALDDSGLE-VTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK08722 157 NIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:PRK08722 237 GMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   361 KAIKH-LFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQewKTEKRFI 439
Cdd:PRK08722 317 KGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KVESMEY 394

                        410
                 ....*....|....*
gi 8923559   440 GLTNSFGFGGTNATL 454
Cdd:PRK08722 395 AICNSFGFGGTNGSL 409
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 42-451 2.15e-124

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 367.52  E-value: 2.15e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT------DFDPTEVMDPKEVKKADRFIQL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK08439  76 GLKAAREAMKDAGFLP-EELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPegEGALRCMAAALKDAGVqpEEISYINAHATSTPLGDAAEN 360
Cdd:PRK08439 235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGN--PKIDYINAHGTSTPYNDKNET 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN---VV 387

                        410
                 ....*....|.
gi 8923559   441 LTNSFGFGGTN 451
Cdd:PRK08439 388 MSNSFGFGGTN 398
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 136-456 1.17e-96

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 294.33  E-value: 1.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   136 HPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHA 215
Cdd:PRK14691  18 HADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   216 VGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQ 293
Cdd:PRK14691  98 IGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALA 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   294 RRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDhAYA 373
Cdd:PRK14691 178 RGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   374 LAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQewkTEKRFIGLTNSFGFGGTNA 452
Cdd:PRK14691 257 LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQ---PHDMTYALSNGFGFAGVNA 333


                 ....
gi 8923559   453 TLCI 456
Cdd:PRK14691 334 SILL 337
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 42-457 2.99e-96

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 299.97  E-value: 2.99e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGqfneqnFVSKSDIKSMSSPTIM 121
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDG------WVAPKLSKRMDKFMLY 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   122 AIGAAELAMKDSGWHPQ--SEADQVATGVAIGMGMIPLEVVSEtALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLK 199
Cdd:PLN02787 203 LLTAGKKALADGGITEDvmKELDKTKCGVLIGSAMGGMKVFND-AIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWM 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   200 GPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGE 278
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGE 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   279 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 358
Cdd:PLN02787 362 GAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLK 441

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   359 ENKAIKHLFKDHAyALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNyVPLKAQEWKTEKRf 438
Cdd:PLN02787 442 EYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK-VLVGPKKERLDIK- 518

                        410
                 ....*....|....*....
gi 8923559   439 IGLTNSFGFGGTNATLCIA 457
Cdd:PLN02787 519 VALSNSFGFGGHNSSILFA 537
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
44-454 1.11e-90

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 281.62  E-value: 1.11e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    44 VVITGIGLVTPLGVGTHLVWDRLIGGESGIVSL---VGEEYkSIPCSVAAYVPRGSDEGqfneqnfVSKSDIKSMSSPTI 120
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLddpFVEEF-DLPVRIGGHLLEEFDHQ-------LTRVELRRMSYLQR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   121 MAIGAAELAMKDSGwhpQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK07910  86 MSTVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   201 PNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARA-LST-NSDPKLACRPFHPKRDGFVMGE 278
Cdd:PRK07910 163 GVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTnNDDPAGACRPFDKDRDGFVFGE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   279 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 358
Cdd:PRK07910 243 GGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   359 ENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVplkAQEWKTEKRF 438
Cdd:PRK07910 323 EGKAINNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVV---AGEPRPGNYR 397

                        410
                 ....*....|....*.
gi 8923559   439 IGLTNSFGFGGTNATL 454
Cdd:PRK07910 398 YAINNSFGFGGHNVAL 413
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
42-456 6.20e-88

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 274.17  E-value: 6.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVG-EEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwDRYDGLNTRLAAPID------DFELPAHYTRKKIRSMGRVSL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   121 MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK09116  76 MATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   201 PNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEG 279
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLVIGEG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   280 AAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGalRCMAAALKDAGVQPEEISYINAHATSTPLGDAAE 359
Cdd:PRK09116 235 AGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   360 NKAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYvpLKAQEWKTEKRF 438
Cdd:PRK09116 313 SQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDY--IMGEAREIDTEY 387

                        410
                 ....*....|....*...
gi 8923559   439 IgLTNSFGFGGTNATLCI 456
Cdd:PRK09116 388 V-MSNNFAFGGINTSLIF 404
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
43-458 3.99e-86

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 268.84  E-value: 3.99e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    43 RVVITGIGLVTPLGvGTHLVWDRLIGGESGIvSLVG--EEYKSIPCSVAAYVPrgsdegqfneqnfvskSDIKSMSSPTI 120
Cdd:PRK05952   3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGI-KLHQpfPELPPLPLGLIGNQP----------------SSLEDLTKTVV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   121 MAigaaelAMKDSGWHPqSEADqvaTGVAIGMG---------MIPLEVVSETALNFQTKGYNKVSpffvpkILVNMAAGQ 191
Cdd:PRK05952  65 TA------ALKDAGLTP-PLTD---CGVVIGSSrgcqgqwekLARQMYQGDDSPDEELDLENWLD------TLPHQAAIA 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnsdpKLACRPFHPKR 271
Cdd:PRK05952 129 AARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQR 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   272 DGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATS 351
Cdd:PRK05952 204 EGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTA 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   352 TPLGDAAENKAIKHLFkdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLdcSEPEFDLNYVpLKAQE 431
Cdd:PRK05952 284 TRLNDQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNFV-RQAQQ 357

                        410       420
                 ....*....|....*....|....*..
gi 8923559   432 WKTEKrfiGLTNSFGFGGTNATLCIAG 458
Cdd:PRK05952 358 SPLQN---VLCLSFGFGGQNAAIALGK 381
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
42-454 4.82e-83

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 261.53  E-value: 4.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVslVGEEYKSI--PCSVAAYVprgsdegQFNEQNFVSKSDIKSMSSPT 119
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMgmRSQVWGNV-------KLDPTGLIDRKVMRFMGDAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   120 IMAIGAAELAMKDSGWhpqsEADQVA---TGVAIGMG-MIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIR 195
Cdd:PRK07967  73 AYAYLAMEQAIADAGL----SEEQVSnprTGLIAGSGgGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   196 YKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAgFSRARALST--NSDPKLACRPFHPKRDG 273
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   274 FVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITApdPEGEGALRCMAAALkdAGVQpEEISYINAHATSTP 353
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTP 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   354 LGDAAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYVPLKAQEW 432
Cdd:PRK07967 303 VGDVKELGAIREVFGDK--SPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDNA 380

                        410       420
                 ....*....|....*....|..
gi 8923559   433 KTEkrfIGLTNSFGFGGTNATL 454
Cdd:PRK07967 381 ELT---TVMSNSFGFGGTNATL 399
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
44-458 2.42e-80

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 255.33  E-value: 2.42e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    44 VVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVprgsdegqfneqNFVsksDIKSMSSPTI--- 120
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFL---PESPFGASALsea 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   121 MAIGAAELAMKDSG--------------------WHPQSEADQvATGVAIGMGMIPLEVVSETalnfqtkgyNKVSPFFv 180
Cdd:PRK06501  78 LARLAAEEALAQAGigkgdfpgplflaappveleWPARFALAA-AVGDNDAPSYDRLLRAARG---------GRFDALH- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   181 PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSD- 259
Cdd:PRK06501 147 ERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDp 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   260 PKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQP 339
Cdd:PRK06501 227 PEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTP 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   340 EEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPE 419
Cdd:PRK06501 307 EQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPA 386

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 8923559   420 FDLNYVPLKAQEWKTEKRfigLTNSFGFGGTNATLCIAG 458
Cdd:PRK06501 387 IPLDVVPNVARDARVTAV---LSNSFGFGGQNASLVLTA 422
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 42-454 3.75e-79

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 251.59  E-value: 3.75e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   42 RRVVITGIGLVTPLGVGTHLV---WDRLIGGESGIVSLVGEEYKSiPCSVAAYVPRGSDEGQFneqnfVSKSDIksMSSP 118
Cdd:cd00828   1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSRF-DRGVAGQIPTGDIPGWD-----AKRTGI--VDRT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFqtkgYNKVSPFFVPK--ILVNMAAGQVSIRY 196
Cdd:cd00828  73 TLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLD----ARAVNPYVSPKwmLSPNTVAGWVNILL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  197 KLK-GPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSTNSD-PKLACRPFHPKRDGF 274
Cdd:cd00828 149 LSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEePEEMSRPFDETRDGF 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  275 VMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPeGEGALRCMAAALKDAGVQPEEISYINAHATSTPL 354
Cdd:cd00828 228 VEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPA 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  355 GDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKT 434
Cdd:cd00828 307 NDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNL 386

                       410       420
                ....*....|....*....|
gi 8923559  435 EKRfIGLTNSFGFGGTNATL 454
Cdd:cd00828 387 KVR-AALVNAFGFGGSNAAL 405
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
198-454 1.76e-73

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 236.28  E-value: 1.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   198 LKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALStnsdpKLACRPFHPKRDGFVMG 277
Cdd:PRK09185 149 LSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS-----PQPCRPFSANRDGINIG 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   278 EGAAVLVLE-EYEHAVQrrariyaeVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 356
Cdd:PRK09185 223 EAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLND 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   357 AAENKAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYvpLKAQEWKTEK 436
Cdd:PRK09185 295 AMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLY--LVENAQALAI 369

                        250
                 ....*....|....*...
gi 8923559   437 RFIgLTNSFGFGGTNATL 454
Cdd:PRK09185 370 RYV-LSNSFAFGGNNCSL 386
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 129-452 9.29e-69

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 224.74  E-value: 9.29e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  129 AMKDSGWHPQSEADQvATGVAIGMGmiplevvSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTA 208
Cdd:cd00833  98 ALEDAGYSPESLAGS-RTGVFVGAS-------SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTA 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  209 CTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnsdPKLACRPFHPKRDGFVMGEGAAVLVLEEY 288
Cdd:cd00833 170 CSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----PDGRCRPFDADADGYVRGEGVGVVVLKRL 245

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  289 EHAVQRRARIYAEVLGYGLS--GDAGHITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHL 366
Cdd:cd00833 246 SDALRDGDRIYAVIRGSAVNqdGRTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKV 323

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  367 F---KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWK--TEKR 437
Cdd:cd00833 324 FggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPTEARPWPapAGPR 403

                       330
                ....*....|....*
gi 8923559  438 FIGLtNSFGFGGTNA 452
Cdd:cd00833 404 RAGV-SSFGFGGTNA 417
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 43-457 5.39e-59

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 199.10  E-value: 5.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    43 RVVITGIGLVTPLGVGTHLVWDRLIGGESGI--VSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvMRRPGRQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSAQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   121 MAIGAAELAMKDSGWHPqseADQVATGVAIGMGMIPLEvvsETALNFQTkgYNKVSPFFVPK-ILVNM---AAGQVSIRY 196
Cdd:PRK07103  83 AALAAAREAWRDAALGP---VDPDRIGLVVGGSNLQQR---EQALVHET--YRDRPAFLRPSyGLSFMdtdLVGLCSEQF 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   197 KLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTN---SDPKLACRPFHPKRDG 273
Cdd:PRK07103 155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDrfaDEPEAACRPFDQDRDG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   274 FVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEgaLRCMAAALKDAGVQPEEISYINAHATSTP 353
Cdd:PRK07103 235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   354 LGDAAENKAIKHLFKDHAYalaVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDcsEP-EFDLNYVPLKAQEW 432
Cdd:PRK07103 313 LGDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLD--EPiDERFRWVGSTAESA 387

                        410       420
                 ....*....|....*....|....*
gi 8923559   433 KTEkrfIGLTNSFGFGGTNATLCIA 457
Cdd:PRK07103 388 RIR---YALSLSFGFGGINTALVLE 409
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 42-291 5.45e-56

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 186.30  E-value: 5.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGE-----EYKSIPCSVA--AYVPRG--SDEGQFNEQNF-VSKSD 111
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGglDDIFDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    112 IKSMSSPTIMAIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMiplEVVSETALNFQTKGYNKVSPFFVPKIlVNMAAGQ 191
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSL-DGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNsDPklaCRPFHPKR 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231

                         250       260
                  ....*....|....*....|
gi 8923559    272 DGFVMGEGAAVLVLEEYEHA 291
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 119-454 3.33e-55

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 186.69  E-value: 3.33e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPkilvnmAAGQVSIRYKL 198
Cdd:cd00825  12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG------ASGQIATPLGI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  199 KGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnsdPKLACRPFHPKRDGFVMGE 278
Cdd:cd00825  86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  279 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 358
Cdd:cd00825 162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  359 ENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTekrf 438
Cdd:cd00825 242 ELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRT---- 315

                       330
                ....*....|....*.
gi 8923559  439 iGLTNSFGFGGTNATL 454
Cdd:cd00825 316 -ALLNGFGLGGTNATL 330
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 42-425 8.74e-55

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 187.57  E-value: 8.74e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrGSDEGQFNEQNFVSKSDiksmsSPTIM 121
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVP-DFDAAEHLPGRLLPQTD-----RMTRL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPF--FVPKILVNmaAGQVSIRYKLK 199
Cdd:cd00832  75 ALAAADWALADAGVDP-AALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsFAWFYAVN--TGQISIRHGMR 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  200 GPNHAVSTACTTGAHAVGDSFRFIAHGdADVMVAGGTDSCISPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEG 279
Cdd:cd00832 152 GPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  280 AAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaghitaPDP---EGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 356
Cdd:cd00832 231 GAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELD 304

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923559  357 AAENKAIKHLFKdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYV 425
Cdd:cd00832 305 RAEAAALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV 371
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 129-452 1.92e-53

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 193.17  E-value: 1.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   129 AMKDSGWHPQSEADQvATGVAIGMGMiplevvsETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTA 208
Cdd:COG3321  102 ALEDAGYDPESLAGS-RTGVFVGASS-------NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   209 CTTGAHAVgdsfrfiaH--------GDADVMVAGGTDSCISPLSLAGFSRARALStnsdPKLACRPFHPKRDGFVMGEGA 280
Cdd:COG3321  174 CSSSLVAV--------HlacqslrsGECDLALAGGVNLMLTPESFILFSKGGMLS----PDGRCRAFDADADGYVRGEGV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDaGH---ITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPLGDA 357
Cdd:COG3321  242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQD-GRsngLTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDP 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   358 AENKAIKHLFKDHAYA---LAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLK 428
Cdd:COG3321  319 IEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGV--AGLikAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTE 396

                        330       340
                 ....*....|....*....|....*.
gi 8923559   429 AQEWKTEK--RFIGLtNSFGFGGTNA 452
Cdd:COG3321  397 LRPWPAGGgpRRAGV-SSFGFGGTNA 421
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 299-414 1.34e-46

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 156.96  E-value: 1.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    299 YAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAY--ALAV 376
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 8923559    377 SSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLD 414
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 181-451 3.73e-35

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 139.76  E-value: 3.73e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     181 PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDp 260
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     261 klaCRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDA--GHITAPDPEGEGalRCMAAALKDAGVQ 338
Cdd:TIGR02813  257 ---IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     339 PEEISYINAHATSTPLGDAAENKAIKHLF---KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDC 415
Cdd:TIGR02813  332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQ 411

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 8923559     416 SEPEFDLNYVPL----KAQEWKTEK----RFIGLTnSFGFGGTN 451
Cdd:TIGR02813  412 PNPKLDIENSPFylntETRPWMQREdgtpRRAGIS-SFGFGGTN 454
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 188-456 2.93e-32

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 123.32  E-value: 2.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  188 AAGQVSIRYKLK-GPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCisplslagfsraralstnsdpklacrp 266
Cdd:cd00327  46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  267 fhpkrdgfVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaGHITAPDPEGEGALRCMAAALKDAGVQPEEISYIN 346
Cdd:cd00327  99 --------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFD-GASMVPAVSGEGLARAARKALEGAGLTPSDIDYVE 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  347 AHATSTPLGDAAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLN-LDCsepefdlnyv 425
Cdd:cd00327 170 AHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTPRePRT---------- 237

                       250       260       270
                ....*....|....*....|....*....|.
gi 8923559  426 plkaqewktekrfiGLTNSFGFGGTNATLCI 456
Cdd:cd00327 238 --------------VLLLGFGLGGTNAAVVL 254
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 204-452 1.77e-27

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 111.27  E-value: 1.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     204 AVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSdpklACRPFHPKRDGFVMGEGAAVL 283
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDG----RCKTFDASADGYVRGEGVGVV 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     284 VLEEYEHAVQRRARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaalkdagvQpeeisyinahatstplgdaaenk 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA----------------Q----------------------- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559     362 aikhlfkdhayaLAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTE 435
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274

                          250
                   ....*....|....*....
gi 8923559     436 --KRFIGLtNSFGFGGTNA 452
Cdd:smart00825 275 grPRRAGV-SSFGFGGTNA 292
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
41-412 3.24e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 64.59  E-value: 3.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559    41 HRRVVITGIGLVTPLGVGTHLVWDRLiggESGIVSLVGEEYKSIPCSVAAYVPRGSDegqfneQNFVSKSDIKSMSspTI 120
Cdd:PRK06519   5 PNDVVITGIGLVSSLGEGLDAHWNAL---SAGRPQPNVDTETFAPYPVHPLPEIDWS------QQIPKRGDQRQME--TW 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   121 MAIG--AAELAMKDSGWHPQSEA----DQVatgVAIGMGMIPLEV----------VSETALNFQTKGYNKVSPFFVPKIL 184
Cdd:PRK06519  74 QRLGtyAAGLALDDAGIKGNEELlstmDMI---VAAGGGERDIAVdtailnearkRNDRGVLLNERLMTELRPTLFLAQL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   185 VNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNsdpklac 264
Cdd:PRK06519 151 SNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKG------- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   265 rPFHP-------KRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEvlgygLSGDAGHITAPDPegeGAL-RCMAAALKDAG 336
Cdd:PRK06519 224 -GWAPvwsrggeDGGGFILGSGGAFLVLESREHAEARGARPYAR-----ISGVESDRARRAP---GDLeASLERLLKPAG 294

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8923559   337 VQPEEISYINAHATSTPLgdAAENKAikhlFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLN 412
Cdd:PRK06519 295 GLAAPTAVISGATGAHPA--TAEEKA----ALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFD 364
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 196-345 2.02e-08

3-oxoacyl-(acyl carrier protein) synthase; Validated


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 55.80  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559   196 YKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDPklacrpfhpkrDGFV 275
Cdd:PRK06147 120 LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFI 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923559   276 MGEGAAVLVLEEYEHAVQRRARIYAevLGYGL--SGDAGHITAPdPEGEGALRCMAAALKDAGVQPEEISYI 345
Cdd:PRK06147 189 PGEAAAAVLLGRPAGGEAPGLPLLG--LGLGRepAPVGESEDLP-LRGDGLTQAIRAALAEAGCGLEDMDYR 257
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 205-296 1.30e-04

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 43.90  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559  205 VSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSC-----ISPLSLAGFSR-ARALSTNSDPKLACRpfhpkRDGFVMGE 278
Cdd:COG0183  84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsrapmLLPKARWGYRMnAKLVDPMINPGLTDP-----YTGLSMGE 158

                        90       100
                ....*....|....*....|....*...
gi 8923559  279 GAAVLVlEEY--------EHAV--QRRA 296
Cdd:COG0183 159 TAENVA-ERYgisreeqdAFALrsHQRA 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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