NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|992319584|ref|NP_001307055|]
View 

monoacylglycerol lipase ABHD6 [Homo sapiens]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-327 3.33e-41

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 143.22  E-value: 3.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  51 RYVHHEDYQFCYSFRGRPGhkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596    5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 131 FVEclKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVcpaglqystdNQFVQRLKElqgsaavekiplipstpeem 210
Cdd:COG0596   82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 211 semlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596  130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 992319584 291 KSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 327
Cdd:COG0596  185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-327 3.33e-41

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 143.22  E-value: 3.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  51 RYVHHEDYQFCYSFRGRPGhkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596    5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 131 FVEclKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVcpaglqystdNQFVQRLKElqgsaavekiplipstpeem 210
Cdd:COG0596   82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 211 semlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596  130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 992319584 291 KSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 327
Cdd:COG0596  185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-313 2.52e-29

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 112.60  E-value: 2.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLVGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  150 GGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGS-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFKV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                         250
                  ....*....|.
gi 992319584  303 NCGHSVVMERP 313
Cdd:pfam00561 235 DAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 62-327 5.45e-29

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 114.66  E-value: 5.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  62 YSFRGrPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875 123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 142 fHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875 200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 222 FKVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875 262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 992319584 289 LAksiANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 327
Cdd:PRK14875 336 LP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 71-324 7.56e-23

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 95.36  E-value: 7.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   71 KPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLVGT 147
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  148 SMGGQVAGVYAAYYPSDVSSLCLV-CPAGLQ--------YSTDNQFVQRLkELQGSAAV----EKIPLIpSTPEEMseml 214
Cdd:TIGR03695  79 SMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF-EQEGLEAFlddwYQQPLF-ASQKNL---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  215 qlcsyvrfkvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKSIA 294
Cdd:TIGR03695 153 ----------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKLIP 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 992319584  295 NCQVELLENCGHSVVMERPRKTAKLIIDFL 324
Cdd:TIGR03695 222 NLTLHIIPNAGHNIHLENPEAFAKILLAFL 251
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-327 3.33e-41

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 143.22  E-value: 3.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  51 RYVHHEDYQFCYSFRGRPGhkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596    5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 131 FVEclKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVcpaglqystdNQFVQRLKElqgsaavekiplipstpeem 210
Cdd:COG0596   82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 211 semlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596  130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 992319584 291 KSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 327
Cdd:COG0596  185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-313 2.52e-29

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 112.60  E-value: 2.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLVGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  150 GGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGS-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFKV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                         250
                  ....*....|.
gi 992319584  303 NCGHSVVMERP 313
Cdd:pfam00561 235 DAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 62-327 5.45e-29

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 114.66  E-value: 5.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  62 YSFRGrPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875 123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 142 fHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875 200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 222 FKVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875 262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 992319584 289 LAksiANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 327
Cdd:PRK14875 336 LP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
60-326 3.26e-25

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 101.23  E-value: 3.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  60 FCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLK-L 137
Cdd:COG2267   17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRaR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 138 NKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAglqYSTDnqfvqrlkelqgsaavekiPLIPSTPEEMSEMLqlc 217
Cdd:COG2267   97 PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA---YRAD-------------------PLLGPSARWLRALR--- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 218 syvrfkvpqqilqglvdvriphnnfyrklfleivseksrysLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA-NC 296
Cdd:COG2267  152 -----------------------------------------LAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSpDV 190

                        250       260       270
                 ....*....|....*....|....*....|.
gi 992319584 297 QVELLENCGHSVVMERPRKTA-KLIIDFLAS 326
Cdd:COG2267  191 ELVLLPGARHELLNEPAREEVlAAILAWLER 221
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 71-324 7.56e-23

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 95.36  E-value: 7.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   71 KPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLVGT 147
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  148 SMGGQVAGVYAAYYPSDVSSLCLV-CPAGLQ--------YSTDNQFVQRLkELQGSAAV----EKIPLIpSTPEEMseml 214
Cdd:TIGR03695  79 SMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF-EQEGLEAFlddwYQQPLF-ASQKNL---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  215 qlcsyvrfkvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKSIA 294
Cdd:TIGR03695 153 ----------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKLIP 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 992319584  295 NCQVELLENCGHSVVMERPRKTAKLIIDFL 324
Cdd:TIGR03695 222 NLTLHIIPNAGHNIHLENPEAFAKILLAFL 251
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
68-329 4.12e-20

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 87.69  E-value: 4.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  68 PGHKPSILMLHGFSAHKdmwlSVVKFLPKNLH-----LVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPF 142
Cdd:COG1647   12 EGGRKGVLLLHGFTGSP----AEMRPLAEALAkagytVYAPRLPGH-GTSPEDLLKTTWEDWLEDVEEAYEILKAGYDKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 143 HLVGTSMGGQVAGVYAAYYPsDVSSLCLVCPAgLQYSTDNQFVQRLkelqGSAAVEKIPLIPSTPEEmsemLQLCSYVRF 222
Cdd:COG1647   87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPA-LKIDDPSAPLLPL----LKYLARSLRGIGSDIED----PEVAEYAYD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 223 KVPQQILQglvdvriphnNFYRklFLEIVSEksryslhqNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVEL-- 300
Cdd:COG1647  157 RTPLRALA----------ELQR--LIREVRR--------DLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELvw 216

                        250       260       270
                 ....*....|....*....|....*....|
gi 992319584 301 LENCGHSVVMERPRKT-AKLIIDFLASVHN 329
Cdd:COG1647  217 LEDSGHVITLDKDREEvAEEILDFLERLAA 246
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 74-319 5.51e-12

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 64.42  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   74 ILMLHGFSAHKDmwlSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSidgQVKRIHQFVECLKlNKKPFHLVGTSMGGQV 153
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGH-GSSSPPPLDLA---DLADLAALLDELG-AARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  154 AgvyAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMsemlqlcsyVRFKVPQQILQGLV 233
Cdd:pfam12697  73 A---LAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGF---------LDDLPADAEWAAAL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  234 DVRIPHNNFYRKLFLEivseksryslhqNMDKIKVPTQIIWGkQDQVLDvSGADMLAKSIANCQVELLENCGHSvVMERP 313
Cdd:pfam12697 141 ARLAALLAALALLPLA------------AWRDLPVPVLVLAE-EDRLVP-ELAQRLLAALAGARLVVLPGAGHL-PLDDP 205


                  ....*.
gi 992319584  314 RKTAKL 319
Cdd:pfam12697 206 EEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 70-312 4.69e-11

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 61.85  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   70 HKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTR--SSLDDLsidgqVKRIHQFVECLKLN--KKP 141
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHgrsDGKRGhvPSFDDY-----VDDLDTFVDKIREEhpGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  142 FHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPA-GLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMS---EMLQLC 217
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPAlKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSrdpEVVAAY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  218 ---SYVRFKVPQQILQGLVDVRIphnnfyrklfleivseksrySLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI- 293
Cdd:pfam12146 158 aadPLVHGGISARTLYELLDAGE--------------------RLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAg 217

                         250       260
                  ....*....|....*....|
gi 992319584  294 -ANCQVELLENCGHSVVMER 312
Cdd:pfam12146 218 sTDKTLKLYPGLYHELLNEP 237
PLN02578 PLN02578
hydrolase
 9-326 5.59e-11

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 62.94  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   9 FVIAGGTLAIPILAFVASFLLWP-SALIRI-------YYWYWRrtlGMQVRYVhhedyqfcysfrgRPGHKPSILMLHGF 80
Cdd:PLN02578  32 IFIFGGIVASGVSVMGSSSASQSvQGLERLpfkkegyNFWTWR---GHKIHYV-------------VQGEGLPIVLIHGF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  81 SAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLddLSIDGQVKRiHQFVECLK-LNKKPFHLVGTSMGGQVAGVYAA 159
Cdd:PLN02578  96 GASAFHWRYNIPELAKKYKVYALDLLGF-GWSDKAL--IEYDAMVWR-DQVADFVKeVVKEPAVLVGNSLGGFTALSTAV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 160 YYPSDVSSLCLVCPAGlqystdnQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQ----LCSYVRFKVPQQILQGLVDV 235
Cdd:PLN02578 172 GYPELVAGVALLNSAG-------QFGSESREKEEAIVVEETVLTRFVVKPLKEWFQrvvlGFLFWQAKQPSRIESVLKSV 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 236 RIPHNN---------------------FYRkLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA 294
Cdd:PLN02578 245 YKDKSNvddylvesitepaadpnagevYYR-LMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYP 323

                        330       340       350
                 ....*....|....*....|....*....|..
gi 992319584 295 NCQVELLEnCGHSVVMERPRKTAKLIIDFLAS 326
Cdd:PLN02578 324 DTTLVNLQ-AGHCPHDEVPEQVNKALLEWLSS 354
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 72-323 8.22e-10

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 58.29  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   72 PSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTrsSLDDLSIDGQVKRIHQFVEclklnkKPFHLVGTSMGG 151
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR--GFGPLSLADMAEAIAAQAP------DPAIWLGWSLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  152 QVAGVYAAYYPSDVSSLCLVC-----------PAGLQYSTDNQFVQRLKElqgsaavekiplipSTPEEMSEMLQL---- 216
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTVAsspcfsaredwPEGIKPDVLTGFQQQLSD--------------DYQRTIERFLALqtlg 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  217 CSYVRFKVpQQILQGLVDVRIPHNnfyrKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANC 296
Cdd:TIGR01738 143 TPTARQDA-RALKQTLLARPTPNV----QVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHS 217

                         250       260
                  ....*....|....*....|....*..
gi 992319584  297 QVELLENCGHSVVMERPRKTAKLIIDF 323
Cdd:TIGR01738 218 ELYIFAKAAHAPFLSHAEAFCALLVAF 244
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 62-325 3.42e-09

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 56.60  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584   62 YSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGH----EGTTRSSLDDLSIDgqvkrihqfVECL-- 135
Cdd:TIGR02427   4 YRLDGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHglsdAPEGPYSIEDLADD---------VLALld 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  136 KLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGlQYSTDNQFVQRLK--ELQGSAAvekipLIPSTPEemsem 213
Cdd:TIGR02427  75 HLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAA-KIGTPESWNARIAavRAEGLAA-----LADAVLE----- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  214 lqlcsyvRFKVPqqilqglvDVRIPHN---NFYRKLFLEivSEKSRYSLH----QNMD------KIKVPTQIIWGKQDQV 280
Cdd:TIGR02427 144 -------RWFTP--------GFREAHParlDLYRNMLVR--QPPDGYAGCcaaiRDADfrdrlgAIAVPTLCIAGDQDGS 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 992319584  281 LDVSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLA 325
Cdd:TIGR02427 207 TPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
68-325 1.38e-08

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 54.64  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  68 PGHKPSILMLHGFSAHKD-MWLSVVKFLPKN-LHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLV 145
Cdd:COG1506   20 GKKYPVVVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGY-GESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGIY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 146 GTSMGGQVAGVYAAYYPSDVSSLCLVCPA---GLQYSTDNQFVQRLKElqgsaavekiplipsTPEEMSEMLQlcsyvrf 222
Cdd:COG1506   99 GHSYGGYMALLAAARHPDRFKAAVALAGVsdlRSYYGTTREYTERLMG---------------GPWEDPEAYA------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 223 kvpqqilqglvdvriphnnfyrklfleivseksRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI--ANCQVEL 300
Cdd:COG1506  157 ---------------------------------ARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALkkAGKPVEL 203

                        250       260
                 ....*....|....*....|....*..
gi 992319584 301 L--ENCGHSVVMERPRKTAKLIIDFLA 325
Cdd:COG1506  204 LvyPGEGHGFSGAGAPDYLERILDFLD 230
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 42-313 2.41e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 54.92  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  42 WRRTLGMQVRYVHhedyqfCYSFRGRPGhKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSI 121
Cdd:PLN02894  83 WFRSASNEPRFIN------TVTFDSKED-APTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKST 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 122 D-GQVKRIHQFVECLKL-NKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKelqgsaavek 199
Cdd:PLN02894 156 EeTEAWFIDSFEEWRKAkNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTK---------- 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 200 ipLIPSTPEEMSEMLQLCSYvrfkVPQQILQGL-----------VDVRIPHNN----------------FYRKLFLEIVS 252
Cdd:PLN02894 226 --FRATWKGAVLNHLWESNF----TPQKIIRGLgpwgpnlvrryTTARFGAHStgdilseeesklltdyVYHTLAAKASG 299

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992319584 253 EK-----------SRYSLHQNMDKIKVPTQIIWGKQDQvLDVSGADMLAKSI-ANCQVELLENCGHSVVMERP 313
Cdd:PLN02894 300 ELclkyifsfgafARKPLLESASEWKVPTTFIYGRHDW-MNYEGAVEARKRMkVPCEIIRVPQGGHFVFLDNP 371
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 71-160 3.41e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 53.69  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  71 KPSILMLHGFSAHKDMWLSVVKFLPKNlHLVCVDMPGHeGTTRssldDLSIDGQVKRIHQFVECLK-LNKKPFHLVGTSM 149
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGH-GGSA----AISVDGFADVSRLLSQTLQsYNILPYWLVGYSL 75

                         90
                 ....*....|.
gi 992319584 150 GGQVAGVYAAY 160
Cdd:PRK11126  76 GGRIAMYYACQ 86
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 70-168 1.19e-05

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.66  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  70 HKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVC-VDMPGHEGTTRSSLDDLsiDGQVKRIHQfveclKLNKKPFHLVGTS 148
Cdd:COG1075    4 TRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYaLNYPSTNGSIEDSAEQL--AAFVDAVLA-----ATGAEKVDLVGHS 76

                         90       100
                 ....*....|....*....|..
gi 992319584 149 MGGQVAGVYAAYY--PSDVSSL 168
Cdd:COG1075   77 MGGLVARYYLKRLggAAKVARV 98
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 62-324 1.60e-05

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 45.68  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  62 YSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTRSSLDDLSIDgqvkrIHQFVEclKL 137
Cdd:COG1073   28 YLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYgesEGEPREEGSPERRD-----ARAAVD--YL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 138 NKKPFH------LVGTSMGGQVAGVYAAYYPsDVSSLCLVCPAglqYSTDNQFVQRLKELQGsaavEKIPLIPSTPeems 211
Cdd:COG1073  101 RTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVILDSPF---TSLEDLAAQRAKEARG----AYLPGVPYLP---- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 212 emlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFleivseksrYSLHQnMDKIKVPTQIIWGKQDQVldVS---GADM 288
Cdd:COG1073  169 ------------------------NVRLASLLNDEF---------DPLAK-IEKISRPLLFIHGEKDEA--VPfymSEDL 212

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 992319584 289 LAKSIANCQVELLENCGHSVVMERPRKTA-KLIIDFL 324
Cdd:COG1073  213 YEAAAEPKELLIVPGAGHVDLYDRPEEEYfDKLAEFF 249
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 67-328 3.75e-04

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 41.38  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584  67 RPGHKPSILMLH--GFSAHkdMWLSVVKFLPKNLHLVCVDMPGHEgtTR------SSLDDLsidgqVKRIHQFVecLKLN 138
Cdd:COG3208    2 RPDARLRLFCFPyaGGSAS--AYRPWAAALPPDIEVLAVQLPGRG--DRlgepplTSLEEL-----ADDLAEEL--APLL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 139 KKPFHLVGTSMGGQVAgvY-------AAYYPSDvssLCLV---CPA-GLQYS-------TDNQFVQRLKELQGsaaveki 200
Cdd:COG3208   71 DRPFALFGHSMGALLA--FelarrleRRGRPLP---AHLFvsgRRApHLPRRrrplhdlSDAELLAELRRLGG------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319584 201 plipsTPEEM---SEMLQLcsyvrfkvpqqILQGLV-DVRIphnnfyrklfLEivseksRYsLHQNMDKIKVPTQIIWGK 276
Cdd:COG3208  139 -----TPEEVladPELLEL-----------FLPILRaDFRL----------LE------TY-RYTPGPPLDCPITALGGD 185

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 992319584 277 QDQvlDVSGADMLA---KSIANCQVELLENcGHSVVMERPRKTAKLIIDFLASVH 328
Cdd:COG3208  186 DDP--LVSPEELAAwreHTTGPFRLRVFPG-GHFFLRDHPAELLALIRAALAALA 237
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH