NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907133032|ref|XP_036017607|]
View 

pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 isoform X2 [Mus musculus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11440907)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to Staphylococcus aureus 4,4'-diaponeurosporene oxygenase

CATH:  3.50.50.60
Gene Ontology:  GO:0016491

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 35-628 1.49e-117

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 359.16  E-value: 1.49e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRP--QICTDLELKKHgLKLH 112
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFE-RPGFRFDVGPSVLTMPGVleRLFRELGLEDY-LELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 113 LRDPySFTPMLEEGtlnrlpRSLLLGTDMAANQKEISQFSRKDAQAFPRYEEFMKRLVLAIDPLLDAAPvdttafqhgsl 192
Cdd:COG1233    82 PLDP-AYRVPFPDG------RALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLYRP----------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 193 lqrlraLSTLKPLLKAgrtlgAQLPQYYEVLTAPISKVLDQRFESEPLKATLATdavIGAMTSPHTPGSGYVLlhHVMGS 272
Cdd:COG1233   144 ------LLSLRDLLRP-----LALARLLRLLLRSLRDLLRRYFKDPRLRALLAG---QALYLGLSPDRTPALY--ALIAY 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 273 LEGTQGAWsYVQGGMGALSDAIASSAATRGASIFTEKTVAKVQVnSEGRAQGVTLQDGEEVRSRVVLSCASPQVTFLELT 352
Cdd:COG1233   208 LEYAGGVW-YPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRLL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 353 PQEWLPGAFVKRISQLDTQSPVTKINVAVDR-LPNFqaapnapgdqpqGHHQcsIHLNcEDtllLHQAFEDAkgglpsqk 431
Cdd:COG1233   286 GEEALPARYRRRLERFRYSPSAFKLYLGLDGpLPGL------------AHHT--IHLS-ED---YEAAFDDI-------- 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 432 wkelpipmdkegmpltigywmqnlrAAGQWlgperrqqkwrrgergARRPMIELCIPSSLDPTLAPPGCHVVSLFTQyTP 511
Cdd:COG1233   340 -------------------------FRGRL----------------PEDPSLYVSIPSLTDPSLAPEGKHTLWVLVP-VP 377

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 512 YTLagGKVWnEQEKNTYADKVFDCIEAYAPGFKRSVLARDILTPPDLERIFRLPGGNIFHGAMSLDQLYFARPvpqhSDY 591
Cdd:COG1233   378 YGL--EDAW-DELKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRP----SNY 450

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1907133032 592 RCPVQGLYLCGSGAHPGGGVMGAA--GRNAAHVVFRDLK 628
Cdd:COG1233   451 RTPIPGLYLVGASTHPGGGVPGVLisGRLAARRILKDLK 489
FAD_binding_2 super family cl46878
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 5-61 7.21e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


The actual alignment was detected with superfamily member PTZ00139:

Pssm-ID: 481218 [Multi-domain]  Cd Length: 617  Bit Score: 39.34  E-value: 7.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133032   5 GRGLIRALHSSPCPTwKRAQSGANGRLKPEYDAVVIGAGHNGLVAAAYLQRLGVNTA 61
Cdd:PTZ00139    1 RFAVPAFNRLTRTFF-SGHLSSAYPVIDHTYDAVVVGAGGAGLRAALGLVELGYKTA 56
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 35-628 1.49e-117

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 359.16  E-value: 1.49e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRP--QICTDLELKKHgLKLH 112
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFE-RPGFRFDVGPSVLTMPGVleRLFRELGLEDY-LELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 113 LRDPySFTPMLEEGtlnrlpRSLLLGTDMAANQKEISQFSRKDAQAFPRYEEFMKRLVLAIDPLLDAAPvdttafqhgsl 192
Cdd:COG1233    82 PLDP-AYRVPFPDG------RALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLYRP----------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 193 lqrlraLSTLKPLLKAgrtlgAQLPQYYEVLTAPISKVLDQRFESEPLKATLATdavIGAMTSPHTPGSGYVLlhHVMGS 272
Cdd:COG1233   144 ------LLSLRDLLRP-----LALARLLRLLLRSLRDLLRRYFKDPRLRALLAG---QALYLGLSPDRTPALY--ALIAY 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 273 LEGTQGAWsYVQGGMGALSDAIASSAATRGASIFTEKTVAKVQVnSEGRAQGVTLQDGEEVRSRVVLSCASPQVTFLELT 352
Cdd:COG1233   208 LEYAGGVW-YPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRLL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 353 PQEWLPGAFVKRISQLDTQSPVTKINVAVDR-LPNFqaapnapgdqpqGHHQcsIHLNcEDtllLHQAFEDAkgglpsqk 431
Cdd:COG1233   286 GEEALPARYRRRLERFRYSPSAFKLYLGLDGpLPGL------------AHHT--IHLS-ED---YEAAFDDI-------- 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 432 wkelpipmdkegmpltigywmqnlrAAGQWlgperrqqkwrrgergARRPMIELCIPSSLDPTLAPPGCHVVSLFTQyTP 511
Cdd:COG1233   340 -------------------------FRGRL----------------PEDPSLYVSIPSLTDPSLAPEGKHTLWVLVP-VP 377

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 512 YTLagGKVWnEQEKNTYADKVFDCIEAYAPGFKRSVLARDILTPPDLERIFRLPGGNIFHGAMSLDQLYFARPvpqhSDY 591
Cdd:COG1233   378 YGL--EDAW-DELKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRP----SNY 450

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1907133032 592 RCPVQGLYLCGSGAHPGGGVMGAA--GRNAAHVVFRDLK 628
Cdd:COG1233   451 RTPIPGLYLVGASTHPGGGVPGVLisGRLAARRILKDLK 489
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 37-628 7.81e-26

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 111.60  E-value: 7.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  37 AVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEIiPGFKFSrasyllslLRPQICTDLELKKHGLKLhlrdp 116
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLED-DGFRFD--------TGPTVITMPEALEELFAL----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 117 ySFTPMLEEGTLNRL-P---------RSLLLGTDMAANQKEISQFSRKDAQAFPRYEEFMKRLV-LAIDPLLdaapvdTT 185
Cdd:TIGR02734  67 -AGRDLADYVELVPLdPfyrlcwedgSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVYrEGYRKLG------YV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 186 AFqhgsllqrlralSTLKPLLKAGR-TLGAQLpqyyevLTAPISKVLDQRFESEPLKATLATDAV-IGamTSPHTPGSGY 263
Cdd:TIGR02734 140 PF------------LSPRDLLRADApQLLALL------AWRSLYSKVARFFSDERLRQAFSFHALfLG--GNPFRTPSIY 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 264 VLLHHvmgsLEGTQGAWsYVQGGMGALSDAIASSAATRGASIFTEKTVAKVQVnSEGRAQGVTLQDGEEVRSRVVLSCAS 343
Cdd:TIGR02734 200 ALISA----LEREWGVW-FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIET-EGGRATAVHLADGERLDADAVVSNAD 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 344 PQVTFLELTPQE--------------WLPGAFVKRISQLDTQspvtkinvavdrlpnfqaapnapGDQPQ-GHHqcsihl 408
Cdd:TIGR02734 274 LHHTYRRLLPNHprrrypaarlsrkrPSPSLFVLYFGLLGVD-----------------------GHWPQlAHH------ 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 409 ncedTLLLhqafedakgglpSQKWKELpipmdkegmpltigywmqnlraagqwlgperrQQKWRRGERGARRPMIELCIP 488
Cdd:TIGR02734 325 ----TLCF------------GPRYKEL--------------------------------FDEIFRKGRLAEDPSLYLHRP 356

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 489 SSLDPTLAPPGCHvvSLFTQY-TPYTLAGGKVWnEQEKNTYADKVFDCIEAYA-PGFKRSVLARDILTPPDLERIFRLPG 566
Cdd:TIGR02734 357 TVTDPSLAPPGCE--SLYVLApVPHLGTADVDW-SVEGPRYRDRILAYLEERAiPGLRDRIVVERTFTPADFRDRYNAWL 433

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133032 567 GNIFHGAMSLDQLYFARPvpqHSDYRcPVQGLYLCGSGAHPGGGVMG--AAGRNAAHVVFRDLK 628
Cdd:TIGR02734 434 GSAFSLEHTLTQSAWFRP---HNRDR-KIDNLYLVGAGTHPGAGVPGvlGSAKATAKLMLGDLA 493
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 46-383 2.03e-14

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 75.99  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  46 GLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEIiPGFKFSRASylLSLLRPQICTDLELKKHGLKLHLRDPYSFTP---M 122
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGGRIRTVRD-DGFLIELGA--MWFHGAQPPLLALLKELGLEDRLVLPDPAPFytvL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 123 LEEGTLNR---LPRSLLLGTDMAanqkeisqfsrkdaqaFPRYEEFMKRLVLAIDPLLdAAPVDTTAFQHGSLLQRLRAL 199
Cdd:pfam01593  80 FAGGRRYPgdfRRVPAGWEGLLE----------------FGRLLSIPEKLRLGLAALA-SDALDEFDLDDFSLAESLLFL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 200 StlkpllkaGRTLGAQlpqyyevltapisKVLDQRFESEPLKATLATDAVIGAMTSPHTPGSGYVLLHHVMGSLEGTqga 279
Cdd:pfam01593 143 G--------RRGPGDV-------------EVWDRLIDPELFAALPFASGAFAGDPSELSAGLALPLLWALLGEGGSL--- 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 280 wSYVQGGMGALSDAIASSAatRGASIFTEKTVAKVQVNSEGraQGVTLQDGEEVRSRVVLsCASPQVTFLELTPQEWLPG 359
Cdd:pfam01593 199 -LLPRGGLGALPDALAAQL--LGGDVRLNTRVRSIDREGDG--VTVTLTDGEVIEADAVI-VTVPLGVLKRILFTPPLPP 272

                         330       340
                  ....*....|....*....|....
gi 1907133032 360 AFVKRISQLDTQsPVTKINVAVDR 383
Cdd:pfam01593 273 EKARAIRNLGYG-PVNKVHLEFDR 295
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 39-83 2.23e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.56  E-value: 2.23e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907133032  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFK 83
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPEFR 187
PTZ00139 PTZ00139
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
 5-61 7.21e-03

Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional


Pssm-ID: 240286 [Multi-domain]  Cd Length: 617  Bit Score: 39.34  E-value: 7.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133032   5 GRGLIRALHSSPCPTwKRAQSGANGRLKPEYDAVVIGAGHNGLVAAAYLQRLGVNTA 61
Cdd:PTZ00139    1 RFAVPAFNRLTRTFF-SGHLSSAYPVIDHTYDAVVVGAGGAGLRAALGLVELGYKTA 56
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 35-628 1.49e-117

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 359.16  E-value: 1.49e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRP--QICTDLELKKHgLKLH 112
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFE-RPGFRFDVGPSVLTMPGVleRLFRELGLEDY-LELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 113 LRDPySFTPMLEEGtlnrlpRSLLLGTDMAANQKEISQFSRKDAQAFPRYEEFMKRLVLAIDPLLDAAPvdttafqhgsl 192
Cdd:COG1233    82 PLDP-AYRVPFPDG------RALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLYRP----------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 193 lqrlraLSTLKPLLKAgrtlgAQLPQYYEVLTAPISKVLDQRFESEPLKATLATdavIGAMTSPHTPGSGYVLlhHVMGS 272
Cdd:COG1233   144 ------LLSLRDLLRP-----LALARLLRLLLRSLRDLLRRYFKDPRLRALLAG---QALYLGLSPDRTPALY--ALIAY 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 273 LEGTQGAWsYVQGGMGALSDAIASSAATRGASIFTEKTVAKVQVnSEGRAQGVTLQDGEEVRSRVVLSCASPQVTFLELT 352
Cdd:COG1233   208 LEYAGGVW-YPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRLL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 353 PQEWLPGAFVKRISQLDTQSPVTKINVAVDR-LPNFqaapnapgdqpqGHHQcsIHLNcEDtllLHQAFEDAkgglpsqk 431
Cdd:COG1233   286 GEEALPARYRRRLERFRYSPSAFKLYLGLDGpLPGL------------AHHT--IHLS-ED---YEAAFDDI-------- 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 432 wkelpipmdkegmpltigywmqnlrAAGQWlgperrqqkwrrgergARRPMIELCIPSSLDPTLAPPGCHVVSLFTQyTP 511
Cdd:COG1233   340 -------------------------FRGRL----------------PEDPSLYVSIPSLTDPSLAPEGKHTLWVLVP-VP 377

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 512 YTLagGKVWnEQEKNTYADKVFDCIEAYAPGFKRSVLARDILTPPDLERIFRLPGGNIFHGAMSLDQLYFARPvpqhSDY 591
Cdd:COG1233   378 YGL--EDAW-DELKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRP----SNY 450

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1907133032 592 RCPVQGLYLCGSGAHPGGGVMGAA--GRNAAHVVFRDLK 628
Cdd:COG1233   451 RTPIPGLYLVGASTHPGGGVPGVLisGRLAARRILKDLK 489
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 37-628 7.81e-26

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 111.60  E-value: 7.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  37 AVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEIiPGFKFSrasyllslLRPQICTDLELKKHGLKLhlrdp 116
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLED-DGFRFD--------TGPTVITMPEALEELFAL----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 117 ySFTPMLEEGTLNRL-P---------RSLLLGTDMAANQKEISQFSRKDAQAFPRYEEFMKRLV-LAIDPLLdaapvdTT 185
Cdd:TIGR02734  67 -AGRDLADYVELVPLdPfyrlcwedgSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVYrEGYRKLG------YV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 186 AFqhgsllqrlralSTLKPLLKAGR-TLGAQLpqyyevLTAPISKVLDQRFESEPLKATLATDAV-IGamTSPHTPGSGY 263
Cdd:TIGR02734 140 PF------------LSPRDLLRADApQLLALL------AWRSLYSKVARFFSDERLRQAFSFHALfLG--GNPFRTPSIY 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 264 VLLHHvmgsLEGTQGAWsYVQGGMGALSDAIASSAATRGASIFTEKTVAKVQVnSEGRAQGVTLQDGEEVRSRVVLSCAS 343
Cdd:TIGR02734 200 ALISA----LEREWGVW-FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIET-EGGRATAVHLADGERLDADAVVSNAD 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 344 PQVTFLELTPQE--------------WLPGAFVKRISQLDTQspvtkinvavdrlpnfqaapnapGDQPQ-GHHqcsihl 408
Cdd:TIGR02734 274 LHHTYRRLLPNHprrrypaarlsrkrPSPSLFVLYFGLLGVD-----------------------GHWPQlAHH------ 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 409 ncedTLLLhqafedakgglpSQKWKELpipmdkegmpltigywmqnlraagqwlgperrQQKWRRGERGARRPMIELCIP 488
Cdd:TIGR02734 325 ----TLCF------------GPRYKEL--------------------------------FDEIFRKGRLAEDPSLYLHRP 356

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 489 SSLDPTLAPPGCHvvSLFTQY-TPYTLAGGKVWnEQEKNTYADKVFDCIEAYA-PGFKRSVLARDILTPPDLERIFRLPG 566
Cdd:TIGR02734 357 TVTDPSLAPPGCE--SLYVLApVPHLGTADVDW-SVEGPRYRDRILAYLEERAiPGLRDRIVVERTFTPADFRDRYNAWL 433

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133032 567 GNIFHGAMSLDQLYFARPvpqHSDYRcPVQGLYLCGSGAHPGGGVMG--AAGRNAAHVVFRDLK 628
Cdd:TIGR02734 434 GSAFSLEHTLTQSAWFRP---HNRDR-KIDNLYLVGAGTHPGAGVPGvlGSAKATAKLMLGDLA 493
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 46-383 2.03e-14

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 75.99  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  46 GLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEIiPGFKFSRASylLSLLRPQICTDLELKKHGLKLHLRDPYSFTP---M 122
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGGRIRTVRD-DGFLIELGA--MWFHGAQPPLLALLKELGLEDRLVLPDPAPFytvL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 123 LEEGTLNR---LPRSLLLGTDMAanqkeisqfsrkdaqaFPRYEEFMKRLVLAIDPLLdAAPVDTTAFQHGSLLQRLRAL 199
Cdd:pfam01593  80 FAGGRRYPgdfRRVPAGWEGLLE----------------FGRLLSIPEKLRLGLAALA-SDALDEFDLDDFSLAESLLFL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 200 StlkpllkaGRTLGAQlpqyyevltapisKVLDQRFESEPLKATLATDAVIGAMTSPHTPGSGYVLLHHVMGSLEGTqga 279
Cdd:pfam01593 143 G--------RRGPGDV-------------EVWDRLIDPELFAALPFASGAFAGDPSELSAGLALPLLWALLGEGGSL--- 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 280 wSYVQGGMGALSDAIASSAatRGASIFTEKTVAKVQVNSEGraQGVTLQDGEEVRSRVVLsCASPQVTFLELTPQEWLPG 359
Cdd:pfam01593 199 -LLPRGGLGALPDALAAQL--LGGDVRLNTRVRSIDREGDG--VTVTLTDGEVIEADAVI-VTVPLGVLKRILFTPPLPP 272

                         330       340
                  ....*....|....*....|....
gi 1907133032 360 AFVKRISQLDTQsPVTKINVAVDR 383
Cdd:pfam01593 273 EKARAIRNLGYG-PVNKVHLEFDR 295
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
39-98 4.35e-10

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 56.00  E-value: 4.35e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907133032  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSR-ASYLLSLLRPQI 98
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYR-VPGYVFDYgAHIFHGSDEPNV 60
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 35-383 3.13e-09

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 59.46  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASyllsllrpqictdlelkkHGlkLHLR 114
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVE-VDGFRIDRGP------------------HS--FLTR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 115 DPYsftpmleegtLNRLPRSLLLGTDMAANQKEISQ-FSRKDAQAFPryeefmkrlvlaidplldAAPVDTTAFQHGSLL 193
Cdd:COG1232    61 DPE----------VLELLRELGLGDELVWPNTRKSYiYYGGKLHPLP------------------QGPLALLRSPLLSLA 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 194 QRLRAL-STLKPLLKAG----------RTLGAQLpqyYEVLTAP-ISKV-------LDQRFESEPLKAT-LATDAVIGAM 253
Cdd:COG1232   113 GKLRALlELLAPRRPPGedeslaefvrRRFGREV---YERLVEPlLEGVyagdpdeLSADWAFPRLKRLeLEHGSLIKGA 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 254 TSPHTPGSGyvllHHVMGSLEgtqgawsyvqGGMGALSDAIAssAATRGASIFTEKTVakVQVNSEGRAQGVTLQDGEEV 333
Cdd:COG1232   190 LALRKGAKA----GEVFGYLR----------GGLGTLVEALA--EALEAGEIRLGTRV--TAIEREGGGWRVTTSDGETI 251

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907133032 334 RSRVVLSCASPQVTfLELTPQewLPGAFVKRISQLDTQSPVTkINVAVDR 383
Cdd:COG1232   252 EADAVVSATPAPAL-ARLLAP--LPPEVAAALAGIPYASVAV-VALGFDR 297
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 33-72 3.00e-08

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 56.41  E-value: 3.00e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907133032  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGA 72
Cdd:COG2072     5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 27-86 1.05e-06

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 51.29  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133032  27 ANGRLKPEYDAV-------VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFKFSR 86
Cdd:COG0493   107 EEGWVKPPPPAPrtgkkvaVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG--LLRYGIPEFRLPK 171
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
35-82 2.08e-06

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 50.12  E-value: 2.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHViGG-AAVTEEI--IPGF 82
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP-GGqLATTKEIenYPGF 50
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 39-83 2.23e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.56  E-value: 2.23e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907133032  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFK 83
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPEFR 187
PRK06370 PRK06370
FAD-containing oxidoreductase;
33-74 4.26e-06

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 49.43  E-value: 4.26e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907133032  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHViGGAAV 74
Cdd:PRK06370    4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLL-GGTCV 44
PRK07233 PRK07233
hypothetical protein; Provisional
 38-402 9.56e-06

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 48.34  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  38 VVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGG-AAVTEeiIPGFK--------FSRASYLLSLLRpqictdlELkkhG 108
Cdd:PRK07233    3 AIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGlAASFE--FGGLPierfyhhiFKSDEALLELLD-------EL---G 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 109 L--KLHLRDPYsfTPMLEEGTLNRLprslllGTdmaanqkeisqfsrkdaqafpryeefmkrlvlaidplldaaPVDTTA 186
Cdd:PRK07233   71 LedKLRWRETK--TGYYVDGKLYPL------GT-----------------------------------------PLELLR 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 187 FQHGSLLQRLR-ALSTL--------KPLLKAG------RTLGaqlPQYYEVLTAPiskVLDQRFESeplkatlATDAV-- 249
Cdd:PRK07233  102 FPHLSLIDKFRlGLLTLlarrikdwRALDKVPaeewlrRWSG---EGVYEVFWEP---LLESKFGD-------YADDVsa 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 250 ------IGAMTSphtpgSGYVLLHHVMGslegtqgawsYVQGGMGALSDAIASSAATRGASIFTEKTVAKVQVNsEGRAQ 323
Cdd:PRK07233  169 awlwsrIKRRGN-----RRYSLFGEKLG----------YLEGGFATLIDALAEAIEARGGEIRLGTPVTSVVID-GGGVT 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 324 GVTLQDGEEVRSRVVlSCASPQVtFLELTPQewLPGAFVKRISQLDTQS----------PVTKI---NVAVDRLP----- 385
Cdd:PRK07233  233 GVEVDGEEEDFDAVI-STAPPPI-LARLVPD--LPADVLARLRRIDYQGvvcmvlklrrPLTDYywlNINDPGAPfggvi 308

                         410       420
                  ....*....|....*....|
gi 1907133032 386 ---NFqaapnAPGDQPQGHH 402
Cdd:PRK07233  309 ehtNL-----VPPERYGGEH 323
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
30-383 3.56e-05

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 46.45  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  30 RLKPEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEI-------------IPGfkfsRASYLLSLLRp 96
Cdd:COG1231     3 RRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFgddglyaelgamrIPP----SHTNLLALAR- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  97 qictdlelkKHGLKLhlrdpysftpmleegtlnrlprslllgtdmaanqkeisqfsrkdaqaFPRYEEFMKRLVlaidpL 176
Cdd:COG1231    78 ---------ELGLPL-----------------------------------------------EPFPNENGNALL-----Y 96

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 177 LDAAPVDTTAFQHgsllqRLRALSTLkpLLKAGRTLGAQLPQYYEVLTA----PISKVLDQRFESEPLKATLATdAVIGA 252
Cdd:COG1231    97 LGGKRVRAGEIAA-----DLRGVAEL--LAKLLRALAAALDPWAHPAAEldreSLAEWLRRNGASPSARRLLGL-LGAGE 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032 253 MTSPHTPGSgyvlLHHV--MGSLEGTQGAWSYVQGGMGALSDAIASSAatrGASIFTEKTVAKVqvnsEGRAQGVTLQ-- 328
Cdd:COG1231   169 YGADPDELS----LLDLlrYAASAGGGAQQFRIVGGMDQLPRALAAEL---GDRIRLGAPVTRI----RQDGDGVTVTtd 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133032 329 DGEEVRSRVVLSCASPQV-TFLELTPQewLPGAFVKRISQLdTQSPVTKINVAVDR 383
Cdd:COG1231   238 DGGTVRADAVIVTVPPSVlRRIEFDPP--LPAAKRAAIQRL-PYGAAIKVFLQFDR 290
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 27-83 4.84e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 46.31  E-value: 4.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133032  27 ANGRLKPEYDAV-------VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFK 83
Cdd:PRK12810  129 EEGWVKPDPPVKrtgkkvaVVGSGPAGLAAADQLARAGHKVTVFERADRIGG--LLRYGIPDFK 190
PLN02576 PLN02576
protoporphyrinogen oxidase
 26-71 6.20e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 45.77  E-value: 6.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907133032  26 GANGRLKPEYDAVVIGAGHNGLVAAAYLQ-RLGVNTAVFERRHVIGG 71
Cdd:PLN02576    4 AEGSAAASSKDVAVVGAGVSGLAAAYALAsKHGVNVLVTEARDRVGG 50
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 34-80 7.34e-05

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 45.46  E-value: 7.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHViGGAAVTEEIIP 80
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL-GGTCLNVGCIP 48
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 34-74 8.76e-05

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 45.21  E-value: 8.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAV 74
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTA 43
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 39-86 1.01e-04

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 45.70  E-value: 1.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907133032   39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFKFSR 86
Cdd:PRK12775   435 ICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG--VLQYGIPSFRLPR 480
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 36-73 1.37e-04

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 44.31  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907133032  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAA 73
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA 38
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
34-74 1.84e-04

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 44.38  E-value: 1.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAV 74
Cdd:PRK05249    5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCT 45
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 33-66 2.25e-04

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 43.77  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907133032  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERR 66
Cdd:COG0654     2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
34-72 2.77e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 43.74  E-value: 2.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGA 72
Cdd:COG0665     2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGA 40
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 34-73 4.41e-04

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 42.07  E-value: 4.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYL-QRLGVNTAVFERRHVIGGAA 73
Cdd:pfam01946  17 ESDVVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGGGA 57
PLN02976 PLN02976
amine oxidase
 38-76 4.83e-04

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 43.32  E-value: 4.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907133032   38 VVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTE 76
Cdd:PLN02976   697 IVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTD 735
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 35-82 8.70e-04

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 42.21  E-value: 8.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVT---------EEIIPGF 82
Cdd:PRK10157    6 FDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVTggrlyahslEHIIPGF 62
PRK10015 PRK10015
oxidoreductase; Provisional
 34-82 1.33e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 41.50  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFER------RHVIGG---AAVTEEIIPGF 82
Cdd:PRK10015    5 KFDAIVVGAGVAGSVAALVMARAGLDVLVIERgdsagcKNMTGGrlyAHTLEAIIPGF 62
GIDA pfam01134
Glucose inhibited division protein A;
36-63 2.55e-03

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 40.61  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907133032  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVF 63
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLI 28
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 34-71 2.79e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 40.51  E-value: 2.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHvIGG 71
Cdd:PRK06416    4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGG 40
PRK07208 PRK07208
hypothetical protein; Provisional
 36-77 2.83e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 40.64  E-value: 2.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907133032  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEE 77
Cdd:PRK07208    6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVT 47
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 35-111 3.21e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 39.99  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133032  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERR-----------HVIGGAAVTEEIIPGFKFSRASYLLSLLRPQICTDLE 103
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcpyggcvlsKALLGAAEAPEIASLWADLYKRKEEVVKKLNNGIEVL 80


                  ....*...
gi 1907133032 104 LKKHGLKL 111
Cdd:pfam07992  81 LGTEVVSI 88
PRK06753 PRK06753
hypothetical protein; Provisional
 39-69 3.69e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 40.06  E-value: 3.69e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907133032  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVI 69
Cdd:PRK06753    5 IIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 34-72 5.29e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 39.74  E-value: 5.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGA 72
Cdd:PRK12844    6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
PRK06481 PRK06481
flavocytochrome c;
31-71 5.36e-03

flavocytochrome c;


Pssm-ID: 180584 [Multi-domain]  Cd Length: 506  Bit Score: 39.82  E-value: 5.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907133032  31 LKPEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGG 71
Cdd:PRK06481   58 LKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGG 98
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 37-113 5.40e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 36.03  E-value: 5.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907133032  37 AVVIGAGHNGLVAAAYLQRLGVNTAVFERRhviggaavteeiipgfkfsraSYLLSLLRPQICTDL--ELKKHGLKLHL 113
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERR---------------------DRLLPGFDPEIAKILqeKLEKNGIEFLL 59
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 34-65 6.03e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.39  E-value: 6.03e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907133032  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFER 65
Cdd:PRK06292    3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEK 34
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 36-74 6.96e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 39.19  E-value: 6.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907133032  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAV 74
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATA 39
PTZ00139 PTZ00139
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
 5-61 7.21e-03

Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional


Pssm-ID: 240286 [Multi-domain]  Cd Length: 617  Bit Score: 39.34  E-value: 7.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133032   5 GRGLIRALHSSPCPTwKRAQSGANGRLKPEYDAVVIGAGHNGLVAAAYLQRLGVNTA 61
Cdd:PTZ00139    1 RFAVPAFNRLTRTFF-SGHLSSAYPVIDHTYDAVVVGAGGAGLRAALGLVELGYKTA 56
 
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