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Conserved domains on  [gi|518801140|ref|WP_019957094|]
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NADPH-dependent 2,4-dienoyl-CoA reductase [Vitreoscilla stercoraria]

Protein Classification

NADPH-dependent 2,4-dienoyl-CoA reductase( domain architecture ID 11554248)

2,4-dienoyl-CoA reductase catalyzes the NADPH-dependent reduction of 2,4 dienoyl-CoA to 3-trans-enoyl-CoA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
9-358 0e+00

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


:

Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 588.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   9 PLPLHKHILRNRIIMGSMHTGFEEHAEGNEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVKWHRLIT 88
Cdd:cd02930    4 PLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHRLIT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  89 DKVHEHDTKICMQILHTGRYAMSRQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGSEGYL 168
Cdd:cd02930   84 DAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSEGYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 169 INQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGASIFNT 248
Cdd:cd02930  164 INQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADILNT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 249 GIGWHEARIPTIATMVPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQWSNKALAKR 328
Cdd:cd02930  244 GIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAAAGR 323
                        330       340       350
                 ....*....|....*....|....*....|
gi 518801140 329 PESINTCIGCNQACLDHIFAGKLTSCLVNP 358
Cdd:cd02930  324 ADEINTCIACNQACLDHIFTGQRASCLVNP 353
PRK11749 super family cl46914
dihydropyrimidine dehydrogenase subunit A; Provisional
362-498 3.90e-18

dihydropyrimidine dehydrogenase subunit A; Provisional


The actual alignment was detected with superfamily member PRK11749:

Pssm-ID: 481254 [Multi-domain]  Cd Length: 457  Bit Score: 87.54  E-value: 3.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 362 HELQLIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqLN---IAktvpgkqEFNETLRYFAHELSQ 438
Cdd:PRK11749 128 TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG-LLrygIP-------EFRLPKDIVDREVER 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518801140 439 LK---VDVRLNAW----ADAAQLQD-FDEIVLASGIH-PRQVNIEGIDHPKVLS---YLQVLR-----DKAHVGNKV 498
Cdd:PRK11749 200 LLklgVEIRTNTEvgrdITLDELRAgYDAVFIGTGAGlPRFLGIPGENLGGVYSavdFLTRVNqavadYDLPVGKRV 276
Pyr_redox_2 super family cl39093
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
375-637 9.66e-14

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.


The actual alignment was detected with superfamily member pfam07992:

Pssm-ID: 476868 [Multi-domain]  Cd Length: 301  Bit Score: 72.35  E-value: 9.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQI-GGQLNIAKTVPGKQEFNETLRYFAH-------ELSQLKVDVRLN 446
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADlykrkeeVVKKLNNGIEVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  447 A-------WADAAQLQD------------FDEIVLASGIHPRQVNIEGIDHP--KVLSYLqvlrdkahvgnkviiigsgg 505
Cdd:pfam07992  81 LgtevvsiDPGAKKVVLeelvdgdgetitYDRLVIATGARPRLPPIPGVELNvgFLVRTL-------------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  506 igfDVAEFLSHQGEDSS-----QSPTlfqqewqidaSLEQAGGLKSIepqltpsVRDITICQRkSGVVGRNLGKTTGWIH 580
Cdd:pfam07992 141 ---DSAEALRLKLLPKRvvvvgGGYI----------GVELAAALAKL-------GKEVTLIEA-LDRLLRAFDEEISAAL 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 518801140  581 RLSLKEKGVNMLGGVTYLKI--DDAGLHVQIGDQiQVLAADHIIICAGQESNRDLQDAL 637
Cdd:pfam07992 200 EKALEKNGVEVRLGTSVKEIigDGDGVEVILKDG-TEIDADLVVVAIGRRPNTELLEAA 257
 
Name Accession Description Interval E-value
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
9-358 0e+00

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 588.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   9 PLPLHKHILRNRIIMGSMHTGFEEHAEGNEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVKWHRLIT 88
Cdd:cd02930    4 PLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHRLIT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  89 DKVHEHDTKICMQILHTGRYAMSRQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGSEGYL 168
Cdd:cd02930   84 DAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSEGYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 169 INQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGASIFNT 248
Cdd:cd02930  164 INQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADILNT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 249 GIGWHEARIPTIATMVPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQWSNKALAKR 328
Cdd:cd02930  244 GIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAAAGR 323
                        330       340       350
                 ....*....|....*....|....*....|
gi 518801140 329 PESINTCIGCNQACLDHIFAGKLTSCLVNP 358
Cdd:cd02930  324 ADEINTCIACNQACLDHIFTGQRASCLVNP 353
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
1-362 8.91e-153

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 446.15  E-value: 8.91e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   1 MPQALLGTPLPLHKHILRNRIIMGSMHTGFEEhAEG--NEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTD 78
Cdd:COG1902    2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGvpTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  79 DEVKWHRLITDKVHEHDTKICMQILHTGRYAMS-----RQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQ 153
Cdd:COG1902   81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPdlpggWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 154 AGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQ 233
Cdd:COG1902  161 AGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 234 LIQRIEHAGASIFNTGIGWHEARiPTIATMVPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARP 313
Cdd:COG1902  241 LAKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRP 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 518801140 314 MLADAQWSNKALAKRPESINTCIGCNQaCLDHIFAGklTSCLVNPFACH 362
Cdd:COG1902  320 LLADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
Oxidored_FMN pfam00724
NADH:flavin oxidoreductase / NADH oxidase family;
6-329 2.86e-82

NADH:flavin oxidoreductase / NADH oxidase family;


Pssm-ID: 395587 [Multi-domain]  Cd Length: 341  Bit Score: 263.54  E-value: 2.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140    6 LGTPLPLHKHILRNRIIMGSMhTGFEEHAEGN---EHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVK 82
Cdd:pfam00724   2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   83 WHRLITDKVHEHDTKICMQILHTGRYAMSR---QPVAPSAIQAPINPARP-------KALSTEEVKQTVQDYIRCAQLAQ 152
Cdd:pfam00724  81 GWRKLTEAVHKNGSKAGVQLWHLGREAPMEyrpDLEVDGPSDPFALGAQEfeiasprYEMSKEEIKQHIQDFVDAAKRAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  153 QAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDnl 232
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAE-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  233 qLIQRIEHAGASIFNTGIGWHEARIpTIATMVPRAAFS------NFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIAD 306
Cdd:pfam00724 239 -TAQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPvrtrqqHNTLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
                         330       340
                  ....*....|....*....|...
gi 518801140  307 AVCLARPMLADAQWSNKALAKRP 329
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKGRP 339
PRK13523 PRK13523
NADPH dehydrogenase NamA; Provisional
17-324 1.95e-51

NADPH dehydrogenase NamA; Provisional


Pssm-ID: 184110 [Multi-domain]  Cd Length: 337  Bit Score: 181.44  E-value: 1.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  17 LRNRIIMGSMHTGFEEHAEG---NEHLAaFYQARAEGGVALIITggispnEAGAVTEGGA------KLTTDDEVKWHRLI 87
Cdd:PRK13523  14 LKNRIVMSPMCMYSSENKDGkvtNFHLI-HYGTRAAGQVGLVIV------EATAVLPEGRisdkdlGIWDDEHIEGLHKL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  88 TDKVHEHDTKICMQILHTGRYAM-SRQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGSEG 166
Cdd:PRK13523  87 VTFIHDHGAKAAIQLAHAGRKAElEGDIVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEIHGAHG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 167 YLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCgdDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGASIF 246
Cdd:PRK13523 167 YLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVW--DGPLFVRISASDYHPGGLTVQDYVQYAKWMKEQGVDLI 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518801140 247 NTGIGwheARIPTIATMVPRAAFsNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQWSNKA 324
Cdd:PRK13523 245 DVSSG---AVVPARIDVYPGYQV-PFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNPYFPRIA 318
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
362-498 3.90e-18

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 87.54  E-value: 3.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 362 HELQLIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqLN---IAktvpgkqEFNETLRYFAHELSQ 438
Cdd:PRK11749 128 TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG-LLrygIP-------EFRLPKDIVDREVER 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518801140 439 LK---VDVRLNAW----ADAAQLQD-FDEIVLASGIH-PRQVNIEGIDHPKVLS---YLQVLR-----DKAHVGNKV 498
Cdd:PRK11749 200 LLklgVEIRTNTEvgrdITLDELRAgYDAVFIGTGAGlPRFLGIPGENLGGVYSavdFLTRVNqavadYDLPVGKRV 276
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
359-490 1.54e-16

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: 82.49  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 359 FACHELQLIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqlniaktvpgkqefneTLRY----F-- 432
Cdd:COG0493  106 FEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG----------------LLRYgipeFrl 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518801140 433 -----AHELSQLK---VDVRLNAW----ADAAQL-QDFDEIVLASGIH-PRQVNIEGIDHPKVLSYLQVLRD 490
Cdd:COG0493  170 pkdvlDREIELIEalgVEFRTNVEvgkdITLDELlEEFDAVFLATGAGkPRDLGIPGEDLKGVHSAMDFLTA 241
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
375-637 9.66e-14

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: 72.35  E-value: 9.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQI-GGQLNIAKTVPGKQEFNETLRYFAH-------ELSQLKVDVRLN 446
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADlykrkeeVVKKLNNGIEVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  447 A-------WADAAQLQD------------FDEIVLASGIHPRQVNIEGIDHP--KVLSYLqvlrdkahvgnkviiigsgg 505
Cdd:pfam07992  81 LgtevvsiDPGAKKVVLeelvdgdgetitYDRLVIATGARPRLPPIPGVELNvgFLVRTL-------------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  506 igfDVAEFLSHQGEDSS-----QSPTlfqqewqidaSLEQAGGLKSIepqltpsVRDITICQRkSGVVGRNLGKTTGWIH 580
Cdd:pfam07992 141 ---DSAEALRLKLLPKRvvvvgGGYI----------GVELAAALAKL-------GKEVTLIEA-LDRLLRAFDEEISAAL 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 518801140  581 RLSLKEKGVNMLGGVTYLKI--DDAGLHVQIGDQiQVLAADHIIICAGQESNRDLQDAL 637
Cdd:pfam07992 200 EKALEKNGVEVRLGTSVKEIigDGDGVEVILKDG-TEIDADLVVVAIGRRPNTELLEAA 257
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
379-412 6.39e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 52.53  E-value: 6.39e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 518801140  379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQ 412
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
378-415 2.05e-07

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 53.75  E-value: 2.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 518801140  378 AVIGAGPAGLACAKTAAERGHHVTLFDAQSQIG--------GQLNI 415
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGkkllisggGRCNL 46
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
375-637 2.97e-05

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 46.94  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQI--------GGQL--------NIAKTV------------------- 419
Cdd:PRK12409   2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAametsfanGGQLsasnaevwNHWATVlkglkwmlrkdaplllnpk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 420 PGKQE---FNETLRYFAH------ELSQLKVDVR--LNAWADAAQLqDFDeivlasgiHPRQvnieGIdhpkvlsyLQVL 488
Cdd:PRK12409  82 PSWHKyswLAEFLAHIPNyrantiETVRLAIAARkhLFDIAEREGI-DFD--------LERR----GI--------LHIY 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 489 RDKAhvgnkviiigsggiGFDVA----EFLSHQG-EDSSQSPTlfqqewqidasleqagGLKSIEPQL---------TPS 554
Cdd:PRK12409 141 HDKA--------------GFDHAkrvnALLAEGGlERRAVTPE----------------EMRAIEPTLtgeyyggyyTPS 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 555 vrditicqrksgvvgrnlgKTTGWIHRLS------LKEKGVNMLGG--VTYLKIDDAGLHVQI----GDQIQVLAADHII 622
Cdd:PRK12409 191 -------------------DSTGDIHKFTtglaaaCARLGVQFRYGqeVTSIKTDGGGVVLTVqpsaEHPSRTLEFDGVV 251
                        330
                 ....*....|....*
gi 518801140 623 ICAGQESnRDLQDAL 637
Cdd:PRK12409 252 VCAGVGS-RALAAML 265
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
369-404 7.53e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 37.49  E-value: 7.53e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 518801140   369 KPAKnskrIAVIGAGPAGLACAKTAAERGHHVTLFD 404
Cdd:smart01002  19 PPAK----VVVIGAGVVGLGAAATAKGLGAEVTVLD 50
 
Name Accession Description Interval E-value
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
9-358 0e+00

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 588.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   9 PLPLHKHILRNRIIMGSMHTGFEEHAEGNEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVKWHRLIT 88
Cdd:cd02930    4 PLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHRLIT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  89 DKVHEHDTKICMQILHTGRYAMSRQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGSEGYL 168
Cdd:cd02930   84 DAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSEGYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 169 INQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGASIFNT 248
Cdd:cd02930  164 INQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADILNT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 249 GIGWHEARIPTIATMVPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQWSNKALAKR 328
Cdd:cd02930  244 GIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAAAGR 323
                        330       340       350
                 ....*....|....*....|....*....|
gi 518801140 329 PESINTCIGCNQACLDHIFAGKLTSCLVNP 358
Cdd:cd02930  324 ADEINTCIACNQACLDHIFTGQRASCLVNP 353
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
1-362 8.91e-153

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 446.15  E-value: 8.91e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   1 MPQALLGTPLPLHKHILRNRIIMGSMHTGFEEhAEG--NEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTD 78
Cdd:COG1902    2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGvpTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  79 DEVKWHRLITDKVHEHDTKICMQILHTGRYAMS-----RQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQ 153
Cdd:COG1902   81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPdlpggWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 154 AGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQ 233
Cdd:COG1902  161 AGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 234 LIQRIEHAGASIFNTGIGWHEARiPTIATMVPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARP 313
Cdd:COG1902  241 LAKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRP 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 518801140 314 MLADAQWSNKALAKRPESINTCIGCNQaCLDHIFAGklTSCLVNPFACH 362
Cdd:COG1902  320 LLADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
8-326 1.08e-113

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 344.56  E-value: 1.08e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   8 TPLPLHKHILRNRIIMGSMHTGF-EEHAEGNEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVKWHRL 86
Cdd:cd02803    2 SPIKIGGLTLKNRIVMAPMTENMaTEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLRK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  87 ITDKVHEHDTKICMQILHTGRYAMS----RQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVM 162
Cdd:cd02803   82 LTEAVHAHGAKIFAQLAHAGRQAQPnltgGPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVEIH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 163 GSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAG 242
Cdd:cd02803  162 GAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEEAG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 243 ASIFNTGIGWHEARIPTIATM-VPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQWS 321
Cdd:cd02803  242 VDALHVSGGSYESPPPIIPPPyVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDLP 321

                 ....*
gi 518801140 322 NKALA 326
Cdd:cd02803  322 NKARE 326
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
9-339 1.91e-86

Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.


Pssm-ID: 240085 [Multi-domain]  Cd Length: 343  Bit Score: 274.49  E-value: 1.91e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   9 PLPLHKHILRNRIIMGSMHTGFEEHAEGNEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVKWHRLIT 88
Cdd:cd04734    4 PLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFRRLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  89 DKVHEHDTKICMQILHTGRYAM---SRQPV-APSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGS 164
Cdd:cd04734   84 EAVHAHGAVIMIQLTHLGRRGDgdgSWLPPlAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGVELQAA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 165 EGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGA- 243
Cdd:cd04734  164 HGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLAAEGLi 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 244 SIFNTGIG---WHEARIPTIATM-VPRAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQ 319
Cdd:cd04734  244 DYVNVSAGsyyTLLGLAHVVPSMgMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAHIADPH 323
                        330       340
                 ....*....|....*....|
gi 518801140 320 WSNKALAKRPESINTCIGCN 339
Cdd:cd04734  324 LVAKAREGREDDIRPCIGCN 343
Oxidored_FMN pfam00724
NADH:flavin oxidoreductase / NADH oxidase family;
6-329 2.86e-82

NADH:flavin oxidoreductase / NADH oxidase family;


Pssm-ID: 395587 [Multi-domain]  Cd Length: 341  Bit Score: 263.54  E-value: 2.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140    6 LGTPLPLHKHILRNRIIMGSMhTGFEEHAEGN---EHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVK 82
Cdd:pfam00724   2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   83 WHRLITDKVHEHDTKICMQILHTGRYAMSR---QPVAPSAIQAPINPARP-------KALSTEEVKQTVQDYIRCAQLAQ 152
Cdd:pfam00724  81 GWRKLTEAVHKNGSKAGVQLWHLGREAPMEyrpDLEVDGPSDPFALGAQEfeiasprYEMSKEEIKQHIQDFVDAAKRAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  153 QAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDnl 232
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAE-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  233 qLIQRIEHAGASIFNTGIGWHEARIpTIATMVPRAAFS------NFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIAD 306
Cdd:pfam00724 239 -TAQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPvrtrqqHNTLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
                         330       340
                  ....*....|....*....|...
gi 518801140  307 AVCLARPMLADAQWSNKALAKRP 329
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKGRP 339
OYE_YqiM_FMN cd02932
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ...
8-320 4.08e-68

Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.


Pssm-ID: 239242 [Multi-domain]  Cd Length: 336  Bit Score: 226.22  E-value: 4.08e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   8 TPLPLHKHILRNRIIMGSMHTGFEEHAEGNE-HLAaFYQARAEGGVALIIT--------GGISPNEAGavteggakLTTD 78
Cdd:cd02932    3 TPLTLRGVTLKNRIVVSPMCQYSAEDGVATDwHLV-HYGSRALGGAGLVIVeatavspeGRITPGDLG--------LWND 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  79 DEVKWHRLITDKVHEHDTKICMQILHTGRYAMSR-----------------QPVAPSAIQAPINPARPKALSTEEVKQTV 141
Cdd:cd02932   74 EQIEALKRIVDFIHSQGAKIGIQLAHAGRKASTAppwegggpllppggggwQVVAPSAIPFDEGWPTPRELTREEIAEVV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 142 QDYIRCAQLAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDL 221
Cdd:cd02932  154 DAFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDW 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 222 VEHGSTWEDNLQLIQRIEHAGASIFNTGIG--WHEARIPT-IATMVPRAafsnftAKLKQASHLPVIATNRINMPDVAEQ 298
Cdd:cd02932  234 VEGGWDLEDSVELAKALKELGVDLIDVSSGgnSPAQKIPVgPGYQVPFA------ERIRQEAGIPVIAVGLITDPEQAEA 307
                        330       340
                 ....*....|....*....|..
gi 518801140 299 LLQDGIADAVCLARPMLADAQW 320
Cdd:cd02932  308 ILESGRADLVALGRELLRNPYW 329
ER_like_FMN cd02931
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ...
9-358 2.34e-67

Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.


Pssm-ID: 239241 [Multi-domain]  Cd Length: 382  Bit Score: 225.85  E-value: 2.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   9 PLPLHKHILRNRIIMGSMHT-GFEEHAEG-NEHLAAFYQARAEGGVALIITG-GISPNEAGAVTEGGAKLTTDDE---VK 82
Cdd:cd02931    4 PIKIGKVEIKNRFAMAPMGPlGLADNDGAfNQRGIDYYVERAKGGTGLIITGvTMVDNEIEQFPMPSLPCPTYNPtafIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  83 WHRLITDKVHEHDTKICMQI-LHTGRYAM-----SRQPVAPSAIQAPINPARP-KALSTEEVKQTVQDYIRCAQLAQQAG 155
Cdd:cd02931   84 TAKEMTERVHAYGTKIFLQLtAGFGRVCIpgflgEDKPVAPSPIPNRWLPEITcRELTTEEVETFVGKFGESAVIAKEAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 156 YDGVEVMG-SEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVL--------------D 220
Cdd:cd02931  164 FDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSVKsyikdlrqgalpgeE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 221 LVEHGSTWEDNLQLIQRIEHAGASIFNTGIG----WHEARIPTIATmvpRAAFSNFTAKLKQASHLPVIATNRINMPDVA 296
Cdd:cd02931  244 FQEKGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPPMYQK---KGMYLPYCKALKEVVDVPVIMAGRMEDPELA 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518801140 297 EQLLQDGIADAVCLARPMLADAQWSNKALAKRPESINTCIGCNQACLDHIFAGKLTSCLVNP 358
Cdd:cd02931  321 SEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
OYE_like_2_FMN cd04733
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ...
6-317 2.05e-58

Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240084 [Multi-domain]  Cd Length: 338  Bit Score: 200.12  E-value: 2.05e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   6 LGTPLPLH-KHILRNRIIMGSMHtgfEEHAEG----NEHLAAFYQARAEGGVALIITGGI-----SPNEAGAVteGGAKL 75
Cdd:cd04733    1 LGQPLTLPnGATLPNRLAKAAMS---ERLADGrglpTPELIRLYRRWAEGGIGLIITGNVmvdprHLEEPGII--GNVVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  76 TTDDEVKWHRLITDKVHEHDTKICMQILHTGRYA---MSRQPVAPSAIQAPINP----ARPKALSTEEVKQTVQDYIRCA 148
Cdd:cd04733   76 ESGEDLEAFREWAAAAKANGALIWAQLNHPGRQSpagLNQNPVAPSVALDPGGLgklfGKPRAMTEEEIEDVIDRFAHAA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 149 QLAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTW 228
Cdd:cd04733  156 RLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 229 EDNLQLIQRIEHA--------GASIFNTGIGWHEaRIPTIAtmvpRAA-FSNFTAKLKQASHLPVIATNRINMPDVAEQL 299
Cdd:cd04733  236 EDALEVVEALEEAgvdlvelsGGTYESPAMAGAK-KESTIA----REAyFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQA 310
                        330
                 ....*....|....*...
gi 518801140 300 LQDGIADAVCLARPMLAD 317
Cdd:cd04733  311 LASGAVDGIGLARPLALE 328
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
17-336 3.01e-55

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 192.04  E-value: 3.01e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  17 LRNRIIMGSM--HTGFEEHAEGNEHLAaFYQARAeGGVALIITGGISPNEAGAVTEGGAKLTTDDEVKWHRLITDKVHEH 94
Cdd:cd04735   13 LKNRFVMAPMttYSSNPDGTITDDELA-YYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGLRKLAQAIKSK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  95 DTKICMQILHTGRYAMSR-----QPVAPSAIQAPINPA-RPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGSEGYL 168
Cdd:cd04735   91 GAKAILQIFHAGRMANPAlvpggDVVSPSAIAAFRPGAhTPRELTHEEIEDIIDAFGEATRRAIEAGFDGVEIHGANGYL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 169 INQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCG----DDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGAS 244
Cdd:cd04735  171 IQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDkhadKDFILGYRFSPEEPEEPGIRMEDTLALVDKLADKGLD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 245 IFNTGIGWHEARIPTIATMVPRaafsnfTAKL---KQASHLPVIATNRINMPDVAEQLLQDGiADAVCLARPMLADAQWS 321
Cdd:cd04735  251 YLHISLWDFDRKSRRGRDDNQT------IMELvkeRIAGRLPLIAVGSINTPDDALEALETG-ADLVAIGRGLLVDPDWV 323
                        330
                 ....*....|....*
gi 518801140 322 NKALAKRPESINTCI 336
Cdd:cd04735  324 EKIKEGREDEINLEI 338
OYE_like_FMN cd02933
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
8-316 3.82e-53

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include 12-oxophytodienoate reductase, pentaerythritol tetranitrate reductase, morphinone reductase, and related enzymes.


Pssm-ID: 239243 [Multi-domain]  Cd Length: 338  Bit Score: 186.14  E-value: 3.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   8 TPLPLHKHILRNRIIMGSMhTGFEEHAEG--NEHLAAFYQARAEGGvaLIITGG--ISPNEAGAVTEGGakLTTDDEVK- 82
Cdd:cd02933    4 SPLKLGNLTLKNRIVMAPL-TRSRADPDGvpTDLMAEYYAQRASAG--LIITEAtqISPQGQGYPNTPG--IYTDEQVEg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  83 WhRLITDKVHEHDTKICMQILHTGRYAMS------RQPVAPSAIQAP---------INPARPKALSTEEVKQTVQDYIRC 147
Cdd:cd02933   79 W-KKVTDAVHAKGGKIFLQLWHVGRVSHPsllpggAPPVAPSAIAAEgkvftpagkVPYPTPRALTTEEIPGIVADFRQA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 148 AQLAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIfRISVLDLVeHGST 227
Cdd:cd02933  158 ARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADRVGI-RLSPFGTF-NDMG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 228 WEDNLQ----LIQRIEHAgasifntGIGW-H--EARiptiATMVPRAAFSNFTAKLKQASHLPVIATNRINmPDVAEQLL 300
Cdd:cd02933  236 DSDPEAtfsyLAKELNKR-------GLAYlHlvEPR----VAGNPEDQPPDFLDFLRKAFKGPLIAAGGYD-AESAEAAL 303
                        330
                 ....*....|....*.
gi 518801140 301 QDGIADAVCLARPMLA 316
Cdd:cd02933  304 ADGKADLVAFGRPFIA 319
PRK13523 PRK13523
NADPH dehydrogenase NamA; Provisional
17-324 1.95e-51

NADPH dehydrogenase NamA; Provisional


Pssm-ID: 184110 [Multi-domain]  Cd Length: 337  Bit Score: 181.44  E-value: 1.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  17 LRNRIIMGSMHTGFEEHAEG---NEHLAaFYQARAEGGVALIITggispnEAGAVTEGGA------KLTTDDEVKWHRLI 87
Cdd:PRK13523  14 LKNRIVMSPMCMYSSENKDGkvtNFHLI-HYGTRAAGQVGLVIV------EATAVLPEGRisdkdlGIWDDEHIEGLHKL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  88 TDKVHEHDTKICMQILHTGRYAM-SRQPVAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQLAQQAGYDGVEVMGSEG 166
Cdd:PRK13523  87 VTFIHDHGAKAAIQLAHAGRKAElEGDIVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEIHGAHG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 167 YLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCgdDFIIIFRISVLDLVEHGSTWEDNLQLIQRIEHAGASIF 246
Cdd:PRK13523 167 YLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVW--DGPLFVRISASDYHPGGLTVQDYVQYAKWMKEQGVDLI 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518801140 247 NTGIGwheARIPTIATMVPRAAFsNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIADAVCLARPMLADAQWSNKA 324
Cdd:PRK13523 245 DVSSG---AVVPARIDVYPGYQV-PFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNPYFPRIA 318
OYE_like_5_FMN cd04747
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ...
6-332 6.24e-50

Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240095 [Multi-domain]  Cd Length: 361  Bit Score: 177.90  E-value: 6.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   6 LGTPLPLHKHILRNRIIMGSMHTGFEEHAEGNEHLAAFYQARAEGGVALIITGGIS-PNEAGAVTEGGAKLTTDDEVKWH 84
Cdd:cd04747    1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAvDHPAASGDPNVPRFHGEDALAGW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  85 RLITDKVHEHDTKICMQILHTGryaMSRQPVAPSAIQAPinPARP-----------KALSTEEVKQTVQDYIRCAQLAQQ 153
Cdd:cd04747   81 KKVVDEVHAAGGKIAPQLWHVG---AMRKLGTPPFPDVP--PLSPsglvgpgkpvgREMTEADIDDVIAAFARAAADARR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 154 AGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWEDNLQ 233
Cdd:cd04747  156 LGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTARLADTPD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 234 ----LIQRIEHAGASIFN----------------TGIGWheAR----IPTIA--TMVPRAAFSNFTAKLKQASHLPViat 287
Cdd:cd04747  236 eleaLLAPLVDAGVDIFHcstrrfwepefegselNLAGW--TKkltgLPTITvgSVGLDGDFIGAFAGDEGASPASL--- 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 518801140 288 nrinmpDVAEQLLQDGIADAVCLARPMLADAQWSNKALAKRPESI 332
Cdd:cd04747  311 ------DRLLERLERGEFDLVAVGRALLSDPAWVAKVREGRLDEL 349
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
8-327 3.45e-45

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 172.43  E-value: 3.45e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   8 TPLPLHKHILRNRIIMGSMHT-GFEEHAEGNEHLAaFYQARAEGGVALIITGGISPNEAGAVTEGGAKLTTDDEVK-WHR 85
Cdd:PRK08255 401 TPFRLRGLTLKNRVVVSPMAMySAVDGVPGDFHLV-HLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEAaWKR 479
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  86 lITDKVHEH-DTKICMQILHTGRYAMSR-------QP--------VAPSAIQAPINPARPKALSTEEVKQTVQDYIRCAQ 149
Cdd:PRK08255 480 -IVDFVHANsDAKIGIQLGHSGRKGSTRlgwegidEPleegnwplISASPLPYLPGSQVPREMTRADMDRVRDDFVAAAR 558
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 150 LAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLVEHGSTWE 229
Cdd:PRK08255 559 RAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGGNTPD 638
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 230 DNLQLIQRIEHAGASIFN--TGIGWHEARiPTIATM--VPraafsnFTAKLKQASHLPVIATNRINMPDVAEQLLQDGIA 305
Cdd:PRK08255 639 DAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYGRMyqTP------FADRIRNEAGIATIAVGAISEADHVNSIIAAGRA 711
                        330       340
                 ....*....|....*....|..
gi 518801140 306 DAVCLARPMLADAQWSNKALAK 327
Cdd:PRK08255 712 DLCALARPHLADPAWTLHEAAE 733
TMADH_HD_FMN cd02929
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ...
5-363 1.15e-44

Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine.


Pssm-ID: 239239 [Multi-domain]  Cd Length: 370  Bit Score: 163.68  E-value: 1.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   5 LLGTPLPLHKHILRNR-------IIMGSMHTGFeehaegnehLAAFYQARAEGGVALIITGGISPNEAGAVT-EGGAKLT 76
Cdd:cd02929    7 ILFEPIKIGPVTARNRfyqvphcNGMGYRKPSA---------QAAMRGIKAEGGWGVVNTEQCSIHPSSDDTpRISARLW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  77 TDDEVKWHRLITDKVHEHDTKICMQILHTGRYAM---SRQ-PVAPSAIQ---APINPARPKALSTEEVKQTVQDYIRCAQ 149
Cdd:cd02929   78 DDGDIRNLAAMTDAVHKHGALAGIELWHGGAHAPnreSREtPLGPSQLPsefPTGGPVQAREMDKDDIKRVRRWYVDAAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 150 LAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIFRISVLDLV--EHGST 227
Cdd:cd02929  158 RARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIgpGGIES 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 228 WEDNLQLiqrIEHAGASI----FNTG--IGWHE-ARIPTIATMVPRAAFsnftakLKQASHLPVIATNRINMPDVAEQLL 300
Cdd:cd02929  238 EGEGVEF---VEMLDELPdlwdVNVGdwANDGEdSRFYPEGHQEPYIKF------VKQVTSKPVVGVGRFTSPDKMVEVV 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518801140 301 QDGIADAVCLARPMLADAQWSNKALAKRPESINTCIGCNqACLDHIFAGKLTSCLVNPFACHE 363
Cdd:cd02929  309 KSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
PRK10605 PRK10605
N-ethylmaleimide reductase; Provisional
6-317 4.83e-37

N-ethylmaleimide reductase; Provisional


Pssm-ID: 182584 [Multi-domain]  Cd Length: 362  Bit Score: 142.17  E-value: 4.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   6 LGTPLPLHKHILRNRIIMGSMhTGFEEHAEGN---EHLAAFYQARAEGGvaLIITGG--ISPNEAGAVteGGAKLTTDDE 80
Cdd:PRK10605   3 LFSPLKVGAITAPNRVFMAPL-TRLRSIEPGDiptPLMAEYYRQRASAG--LIISEAtqISAQAKGYA--GAPGLHSPEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  81 VKWHRLITDKVHEHDTKICMQILHTGRYAMS------RQPVAPSAIQAPI---------NPAR-----PKALSTEEVKQT 140
Cdd:PRK10605  78 IAAWKKITAGVHAEGGHIAVQLWHTGRISHAslqpggQAPVAPSAINAGTrtslrdengQAIRvetstPRALELEEIPGI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 141 VQDYIRCAQLAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFIIIfRISVL- 219
Cdd:PRK10605 158 VNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADRIGI-RISPLg 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 220 --DLVEHGSTWEDN-LQLIQRIEhagasifNTGIGWHEARIPTIATMVPRAafSNFTAKLKQASHLPVIATNRINmPDVA 296
Cdd:PRK10605 237 tfNNVDNGPNEEADaLYLIEQLG-------KRGIAYLHMSEPDWAGGEPYS--DAFREKVRARFHGVIIGAGAYT-AEKA 306
                        330       340
                 ....*....|....*....|.
gi 518801140 297 EQLLQDGIADAVCLARPMLAD 317
Cdd:PRK10605 307 ETLIGKGLIDAVAFGRDYIAN 327
PLN02411 PLN02411
12-oxophytodienoate reductase
1-217 1.10e-25

12-oxophytodienoate reductase


Pssm-ID: 178033 [Multi-domain]  Cd Length: 391  Bit Score: 109.56  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140   1 MPQALLGTPLPLHKHILRNRIIMGSMHTGFEEHAEGNEHLAAFYQARAEGGvALIITGG--ISPNEAGAVTEGGakLTTD 78
Cdd:PLN02411   7 NSNETLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGtlISPTAPGFPHVPG--IYSD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  79 DEVKWHRLITDKVHEHDTKICMQILHTGRYAMS-RQP--VAP-SAIQAPINP--------------ARPKALSTEEVKQT 140
Cdd:PLN02411  84 EQVEAWKKVVDAVHAKGSIIFCQLWHVGRASHQvYQPggAAPiSSTNKPISErwrilmpdgsygkyPKPRALETSEIPEV 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518801140 141 VQDYIRCAQLAQQAGYDGVEVMGSEGYLINQFIAQRTNQRDDEYGGSLENRHRFATEIVHGIRQTCGDDFiIIFRIS 217
Cdd:PLN02411 164 VEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGVRVS 239
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
362-498 3.90e-18

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 87.54  E-value: 3.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 362 HELQLIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqLN---IAktvpgkqEFNETLRYFAHELSQ 438
Cdd:PRK11749 128 TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG-LLrygIP-------EFRLPKDIVDREVER 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518801140 439 LK---VDVRLNAW----ADAAQLQD-FDEIVLASGIH-PRQVNIEGIDHPKVLS---YLQVLR-----DKAHVGNKV 498
Cdd:PRK11749 200 LLklgVEIRTNTEvgrdITLDELRAgYDAVFIGTGAGlPRFLGIPGENLGGVYSavdFLTRVNqavadYDLPVGKRV 276
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
359-490 1.54e-16

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: 82.49  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 359 FACHELQLIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqlniaktvpgkqefneTLRY----F-- 432
Cdd:COG0493  106 FEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG----------------LLRYgipeFrl 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518801140 433 -----AHELSQLK---VDVRLNAW----ADAAQL-QDFDEIVLASGIH-PRQVNIEGIDHPKVLSYLQVLRD 490
Cdd:COG0493  170 pkdvlDREIELIEalgVEFRTNVEvgkdITLDELlEEFDAVFLATGAGkPRDLGIPGEDLKGVHSAMDFLTA 241
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
369-498 1.72e-14

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 76.84  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 369 KPAKNS-KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIAktVPG--------KQEFNETLRyfahelsqL 439
Cdd:PRK12771 131 APAPDTgKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYG--IPAyrlprevlDAEIQRILD--------L 200
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 440 KVDVRLNAW----ADAAQLQ-DFDEIVLASGIH-PRQVNIEGIDHPKVLSYLQVLR-----DKAHVGNKV 498
Cdd:PRK12771 201 GVEVRLGVRvgedITLEQLEgEFDAVFVAIGAQlGKRLPIPGEDAAGVLDAVDFLRavgegEPPFLGKRV 270
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
375-637 9.66e-14

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: 72.35  E-value: 9.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQI-GGQLNIAKTVPGKQEFNETLRYFAH-------ELSQLKVDVRLN 446
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADlykrkeeVVKKLNNGIEVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  447 A-------WADAAQLQD------------FDEIVLASGIHPRQVNIEGIDHP--KVLSYLqvlrdkahvgnkviiigsgg 505
Cdd:pfam07992  81 LgtevvsiDPGAKKVVLeelvdgdgetitYDRLVIATGARPRLPPIPGVELNvgFLVRTL-------------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  506 igfDVAEFLSHQGEDSS-----QSPTlfqqewqidaSLEQAGGLKSIepqltpsVRDITICQRkSGVVGRNLGKTTGWIH 580
Cdd:pfam07992 141 ---DSAEALRLKLLPKRvvvvgGGYI----------GVELAAALAKL-------GKEVTLIEA-LDRLLRAFDEEISAAL 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 518801140  581 RLSLKEKGVNMLGGVTYLKI--DDAGLHVQIGDQiQVLAADHIIICAGQESNRDLQDAL 637
Cdd:pfam07992 200 EKALEKNGVEVRLGTSVKEIigDGDGVEVILKDG-TEIDADLVVVAIGRRPNTELLEAA 257
gltD PRK12810
glutamate synthase subunit beta; Reviewed
375-477 1.46e-11

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 67.11  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQL--NIAktvpgkqEFNETLRYFAHELSQLK---VDVRLNAWA 449
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLryGIP-------DFKLEKEVIDRRIELMEaegIEFRTNVEV 216
                         90       100       110
                 ....*....|....*....|....*....|....
gi 518801140 450 ----DAAQL-QDFDEIVLASGI-HPRQVNIEGID 477
Cdd:PRK12810 217 gkdiTAEELlAEYDAVFLGTGAyKPRDLGIPGRD 250
PRK12831 PRK12831
putative oxidoreductase; Provisional
338-483 2.38e-10

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 63.11  E-value: 2.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 338 CNQACL-----DHIFAGKLTSCLVNPFACHELQLIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQ 412
Cdd:PRK12831  99 CEGKCVlgikgEPVAIGKLERFVADWARENGIDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGV 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 413 LniaktVPGKQEF---NETLryFAHELSQLK---VDVRLN-------AWADAAQLQDFDEIVLASGIH-PRQVNIEGIDH 478
Cdd:PRK12831 179 L-----VYGIPEFrlpKETV--VKKEIENIKklgVKIETNvvvgktvTIDELLEEEGFDAVFIGSGAGlPKFMGIPGENL 251

                 ....*
gi 518801140 479 PKVLS 483
Cdd:PRK12831 252 NGVFS 256
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
368-488 5.20e-10

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 61.54  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 368 QKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLniAKTVPGKQEFNETLRYFAHELSQLKVDVRLN- 446
Cdd:PRK12770  12 EKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLM--LFGIPEFRIPIERVREGVKELEEAGVVFHTRt 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518801140 447 -AWADAAQ------------------LQDFDEIVLASGI-HPRQVNIEGIDHPKVLSYLQVL 488
Cdd:PRK12770  90 kVCCGEPLheeegdefverivsleelVKKYDAVLIATGTwKSRKLGIPGEDLPGVYSALEYL 151
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
372-483 7.04e-10

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 62.45  E-value: 7.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 372 KNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLniaktVPGKQEFNETLRYFAHELSQLK-------VDVR 444
Cdd:PRK12778 429 KNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVL-----KYGIPEFRLPKKIVDVEIENLKklgvkfeTDVI 503
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 518801140 445 LNAWADAAQL--QDFDEIVLASGIH-PRQVNIEGIDHPKVLS 483
Cdd:PRK12778 504 VGKTITIEELeeEGFKGIFIASGAGlPNFMNIPGENSNGVMS 545
PRK13984 PRK13984
putative oxidoreductase; Provisional
368-489 7.89e-10

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 62.09  E-value: 7.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 368 QKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIAktVPGKQEFNETLRYFAHELSQLKVDVRLNA 447
Cdd:PRK13984 277 DEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHLNT 354
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518801140 448 WA--DAA--QL-QDFDEIVLASGIH-PRQVNIEGIDHPKVLSYLQVLR 489
Cdd:PRK13984 355 RVgkDIPleELrEKHDAVFLSTGFTlGRSTRIPGTDHPDVIQALPLLR 402
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
374-456 1.04e-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: 61.00  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqlnIAKTVpgkqEFNE-TLRYFAHelSQLKVDVRLNAWADAA 452
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG---LIRTV----EVDGfRIDRGPH--SFLTRDPEVLELLREL 71

                 ....
gi 518801140 453 QLQD 456
Cdd:COG1232   72 GLGD 75
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
372-498 2.09e-09

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 60.51  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 372 KNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIAktVPGKQEFNETLRYFAHELSQLKVDVRLNAW--- 448
Cdd:PRK12814 191 KSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYG--IPRFRLPESVIDADIAPLRAMGAEFRFNTVfgr 268
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518801140 449 -ADAAQLQ-DFDEIVLASGIH-PRQVNIEGIDHPKVLSYLQVLRDKA-----HVGNKV 498
Cdd:PRK12814 269 dITLEELQkEFDAVLLAVGAQkASKMGIPGEELPGVISGIDFLRNVAlgtalHPGKKV 326
PRK07233 PRK07233
hypothetical protein; Provisional
376-411 2.95e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 59.52  E-value: 2.95e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 518801140 376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
379-412 6.39e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 52.53  E-value: 6.39e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 518801140  379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQ 412
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
374-411 1.65e-08

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 57.17  E-value: 1.65e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
366-421 2.70e-08

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 56.79  E-value: 2.70e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518801140 366 LIQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLN-IAKTVPG 421
Cdd:COG1148  132 LEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFPG 188
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
378-415 2.93e-08

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 56.21  E-value: 2.93e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518801140 378 AVIGAGPAGLACAKTAAERGHHVTLFDAQSQIG--------GQLNI 415
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGrkilisggGRCNF 46
PRK07208 PRK07208
hypothetical protein; Provisional
373-419 3.87e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 56.44  E-value: 3.87e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 518801140 373 NSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGqlnIAKTV 419
Cdd:PRK07208   3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG---ISRTV 46
HI0933_like pfam03486
HI0933-like protein;
375-416 4.66e-08

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 55.66  E-value: 4.66e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 518801140  375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIA 416
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILIS 42
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
375-469 5.33e-08

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 55.86  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAqsqiggqlniaktvpgkqefNETLRYFAHELSQLKVDVRLNAWaDAAQL 454
Cdd:COG0771    5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDD--------------------RPAPELAAAELEAPGVEVVLGEH-PEELL 63
                         90
                 ....*....|....*
gi 518801140 455 QDFDEIVLASGIHPR 469
Cdd:COG0771   64 DGADLVVKSPGIPPD 78
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
372-411 6.50e-08

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 55.63  E-value: 6.50e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 518801140 372 KNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:COG1233    1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
375-411 6.75e-08

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 54.88  E-value: 6.75e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
373-411 1.54e-07

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 54.16  E-value: 1.54e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 518801140 373 NSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:COG1231    6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
377-480 1.65e-07

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 53.59  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 377 IAVIGAGPAGLACAKTAAERGHHVTLFDAqSQIGGQLNIAKTV---PG---------------KQ--EFNETLRY----- 431
Cdd:COG0492    3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKEIenyPGfpegisgpelaerlrEQaeRFGAEILLeevts 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518801140 432 --FAHELSQLKVDVRLNAWADAaqlqdfdeIVLASGIHPRQVNIEGIDHPK 480
Cdd:COG0492   82 vdKDDGPFRVTTDDGTEYEAKA--------VIIATGAGPRKLGLPGEEEFE 124
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
378-415 2.05e-07

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 53.75  E-value: 2.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 518801140  378 AVIGAGPAGLACAKTAAERGHHVTLFDAQSQIG--------GQLNI 415
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGkkllisggGRCNL 46
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
374-494 2.26e-07

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 53.61  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERGHH--VTLFDAQSqiggQLN-----IAKTVPGKQEFNETLRYFAHELSQLKVDVRLN 446
Cdd:COG1251    1 KMRIVIIGAGMAGVRAAEELRKLDPDgeITVIGAEP----HPPynrppLSKVLAGETDEEDLLLRPADFYEENGIDLRLG 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 447 AWA---DAAQ----LQD-----FDEIVLASGIHPRQVNIEGIDHPKVLsylqVLRDKAHV 494
Cdd:COG1251   77 TRVtaiDRAArtvtLADgetlpYDKLVLATGSRPRVPPIPGADLPGVF----TLRTLDDA 132
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
372-413 2.74e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 53.98  E-value: 2.74e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 518801140 372 KNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQL 413
Cdd:PRK12769 325 KSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLL 366
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
367-488 4.22e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 53.11  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 367 IQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIAktVPGKQEFNETLRYFAHELSQLKVDVRLN 446
Cdd:PRK12809 303 VSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG--IPPFKLDKTVLSQRREIFTAMGIDFHLN 380
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518801140 447 AW----ADAAQL-QDFDEIVLASGIHP-RQVNIEGIDHPKVLSYLQVL 488
Cdd:PRK12809 381 CEigrdITFSDLtSEYDAVFIGVGTYGmMRADLPHEDAPGVIQALPFL 428
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
374-411 1.47e-06

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 50.88  E-value: 1.47e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERgHHVTLFDAQSQIGG 411
Cdd:COG2907    3 RMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
21-312 3.05e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 48.35  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  21 IIMGSMHTGfeehaeGNEHLAAFYQARAEGGVALIITGGISPNEAGAVTEGGAKlttddevkwhrlITDKVHEHDTKICM 100
Cdd:cd04722    1 VILALLAGG------PSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV------------LKEVAAETDLPLGV 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 101 QILHTGRYAmsrqpvapsaiqapinparpkalsteevkqtvqDYIRCAQLAQQAGYDGVEVMGSEGYLInqfiaqrtnqr 180
Cdd:cd04722   63 QLAINDAAA---------------------------------AVDIAAAAARAAGADGVEIHGAVGYLA----------- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 181 ddeyggslenrhRFATEIVHGIRQTcGDDFIIIFRISVLDLVEHGstwednlqliqRIEHAGASIFNTGIGWHEARIPTI 260
Cdd:cd04722   99 ------------REDLELIRELREA-VPDVKVVVKLSPTGELAAA-----------AAEEAGVDEVGLGNGGGGGGGRDA 154
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518801140 261 AtmvprAAFSNFTAKLKQASHLPVIATNRINMPDVAEQLLQDGiADAVCLAR 312
Cdd:cd04722  155 V-----PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
376-447 3.50e-06

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: 45.27  E-value: 3.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518801140  376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNiaktvpgkqefNETLRYFAHELSQLKVDVRLNA 447
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFD-----------PEIAKILQEKLEKNGIEFLLNT 61
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
400-630 4.55e-06

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 49.04  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 400 VTLFDAQSQIGGQLN-IAKTVPGKQEFNETLRYFAHE-LSQLKVDVRLNAWA---DAAQ----LQD-----FDEIVLASG 465
Cdd:COG0446    8 ITVIEKGPHHSYQPCgLPYYVGGGIKDPEDLLVRTPEsFERKGIDVRTGTEVtaiDPEAktvtLRDgetlsYDKLVLATG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 466 IHPRQVNIEGIDHPKVLS-----YLQVLRD--KAHVGNKVIIIGSGGIGFDVAEFLSHQGedssqsptlfqqewqidasl 538
Cdd:COG0446   88 ARPRPPPIPGLDLPGVFTlrtldDADALREalKEFKGKRAVVIGGGPIGLELAEALRKRG-------------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 539 eqagglksiepqltpsvRDITICQRKSGVVGRNLGKTTGWIHRLsLKEKGVNMLGGVTYLKID-DAGLHVQIGDQiQVLA 617
Cdd:COG0446  148 -----------------LKVTLVERAPRLLGVLDPEMAALLEEE-LREHGVELRLGETVVAIDgDDKVAVTLTDG-EEIP 208
                        250
                 ....*....|...
gi 518801140 618 ADHIIICAGQESN 630
Cdd:COG0446  209 ADLVVVAPGVRPN 221
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
377-489 6.94e-06

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: 48.93  E-value: 6.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 377 IAVIGAGPAGLACAKTAAERGHHVTLFDaQSQIGG------------------------------------QLNIAKTVP 420
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGGtclnvgcipskallhaaevahearhaaefgisagapSVDWAALMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 421 GKQEFNETLRYFAHE-LSQLKVDVrLNAWA---DAAQLQ-------DFDEIVLASGIHPRQVNIEGIDHPKVLSYLQVLR 489
Cdd:COG1249   85 RKDKVVDRLRGGVEElLKKNGVDV-IRGRArfvDPHTVEvtggetlTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALE 163
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
370-411 8.07e-06

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 48.70  E-value: 8.07e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 518801140 370 PAKN---SKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:PLN02172   3 PAQNpinSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
376-411 9.23e-06

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: 48.71  E-value: 9.23e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 518801140 376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:COG2072    8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
376-411 1.88e-05

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: 47.39  E-value: 1.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 518801140  376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
371-465 2.02e-05

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 47.11  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 371 AKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNiaktvpgkQEFNETLryfAHELSQLKVDVRLNAWAD 450
Cdd:COG0446  121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLD--------PEMAALL---EEELREHGVELRLGETVV 189
                         90
                 ....*....|....*
gi 518801140 451 AAQLQDFDEIVLASG 465
Cdd:COG0446  190 AIDGDDKVAVTLTDG 204
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
374-461 2.60e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 46.82  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQsQIG--------GQLNIAKTVPGKQEFNETLRYFAHELSQL------ 439
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGsgasgrnaGQLRPGLAALADRALVRLAREALDLWRELaaelgi 80
                         90       100
                 ....*....|....*....|....*.
gi 518801140 440 KVDVR----LNAWADAAQLQDFDEIV 461
Cdd:COG0665   81 DCDFRrtgvLYLARTEAELAALRAEA 106
PLN02976 PLN02976
amine oxidase
375-412 2.90e-05

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 47.55  E-value: 2.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 518801140  375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQ 412
Cdd:PLN02976  694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
375-637 2.97e-05

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 46.94  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQI--------GGQL--------NIAKTV------------------- 419
Cdd:PRK12409   2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAametsfanGGQLsasnaevwNHWATVlkglkwmlrkdaplllnpk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 420 PGKQE---FNETLRYFAH------ELSQLKVDVR--LNAWADAAQLqDFDeivlasgiHPRQvnieGIdhpkvlsyLQVL 488
Cdd:PRK12409  82 PSWHKyswLAEFLAHIPNyrantiETVRLAIAARkhLFDIAEREGI-DFD--------LERR----GI--------LHIY 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 489 RDKAhvgnkviiigsggiGFDVA----EFLSHQG-EDSSQSPTlfqqewqidasleqagGLKSIEPQL---------TPS 554
Cdd:PRK12409 141 HDKA--------------GFDHAkrvnALLAEGGlERRAVTPE----------------EMRAIEPTLtgeyyggyyTPS 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 555 vrditicqrksgvvgrnlgKTTGWIHRLS------LKEKGVNMLGG--VTYLKIDDAGLHVQI----GDQIQVLAADHII 622
Cdd:PRK12409 191 -------------------DSTGDIHKFTtglaaaCARLGVQFRYGqeVTSIKTDGGGVVLTVqpsaEHPSRTLEFDGVV 251
                        330
                 ....*....|....*
gi 518801140 623 ICAGQESnRDLQDAL 637
Cdd:PRK12409 252 VCAGVGS-RALAAML 265
PRK13748 PRK13748
putative mercuric reductase; Provisional
376-422 7.76e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.91  E-value: 7.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 518801140 376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAqSQIGGQ-LNIAkTVPGK 422
Cdd:PRK13748 100 HVAVIGSGGAAMAAALKAVEQGARVTLIER-GTIGGTcVNVG-CVPSK 145
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
369-447 1.14e-04

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: 44.62  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  369 KPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQlniaktvpgkqeFNETLRYFAHE-LSQLKVDVRLNA 447
Cdd:pfam07992 147 RLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA------------FDEEISAALEKaLEKNGVEVRLGT 214
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
375-410 1.16e-04

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 45.22  E-value: 1.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIG 410
Cdd:PRK01747 261 RDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
379-411 1.38e-04

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: 44.96  E-value: 1.38e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 518801140  379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:TIGR02734   3 VIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
371-469 1.46e-04

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 44.75  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 371 AKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQI-GGQLniaktvpgkqefNETL-RYFAHELSQLKVDVRLNA- 447
Cdd:COG1251  139 LAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlPRQL------------DEEAgALLQRLLEALGVEVRLGTg 206
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 518801140 448 --------WADAAQLQD-----FDEIVLASGIHPR 469
Cdd:COG1251  207 vteiegddRVTGVRLADgeelpADLVVVAIGVRPN 241
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
377-413 3.37e-04

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: 43.43  E-value: 3.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 518801140  377 IAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQL 413
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
376-403 3.45e-04

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 42.15  E-value: 3.45e-04
                         10        20
                 ....*....|....*....|....*....
gi 518801140 376 RIAVIGA-GPAGLACAKTAAERGHHVTLF 403
Cdd:COG2910    1 KIAVIGAtGRVGSLIVREALARGHEVTAL 29
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
382-410 3.60e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.03  E-value: 3.60e-04
                         10        20
                 ....*....|....*....|....*....
gi 518801140 382 AGPAGLACAKTAAERGHHVTLFDAQSQIG 410
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
PRK07251 PRK07251
FAD-containing oxidoreductase;
367-476 3.73e-04

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 43.58  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 367 IQKPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIggqlnIAKTVPGKQEFNEtlRYFAHELSQLKVDVRLN 446
Cdd:PRK07251 150 IQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI-----LPREEPSVAALAK--QYMEEDGITFLLNAHTT 222
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 518801140 447 AWADAA---------QLQDFDEIVLASGihpRQVNIEGI 476
Cdd:PRK07251 223 EVKNDGdqvlvvtedETYRFDALLYATG---RKPNTEPL 258
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
376-410 5.69e-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: 42.62  E-value: 5.69e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 518801140 376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIG 410
Cdd:COG0654    5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
377-413 7.17e-04

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 42.60  E-value: 7.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 518801140  377 IAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQL 413
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
379-472 1.14e-03

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 42.15  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140  379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQ--------IGGQLNIAKTVPGKqefnetLRYFAHELSQLKVDVRLNAWAD 450
Cdd:TIGR01438   7 VIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKK------LMHQAALLGQALKDSRNYGWKV 80
                          90       100
                  ....*....|....*....|...
gi 518801140  451 AAQLQ-DFDEIVLASGIHPRQVN 472
Cdd:TIGR01438  81 EETVKhDWKRLVEAVQNHIGSLN 103
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
371-406 1.25e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 41.81  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 518801140 371 AKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQ 406
Cdd:PRK07494   4 EKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPE 39
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
355-413 1.31e-03

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 42.13  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518801140 355 LVNPFACHELQLIQKP--AKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQL 413
Cdd:PRK12779 285 LVNPNANERFAGRISPwaAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVL 345
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
375-414 1.59e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 41.44  E-value: 1.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 518801140  375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLN 414
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLN 40
PRK09126 PRK09126
FAD-dependent hydroxylase;
377-407 1.85e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 41.08  E-value: 1.85e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 518801140 377 IAVIGAGPAGLACAKTAAERGHHVTLFDAQS 407
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQP 36
PLN02487 PLN02487
zeta-carotene desaturase
376-412 2.14e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 41.32  E-value: 2.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 518801140 376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQ 412
Cdd:PLN02487  77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGK 113
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
379-411 2.66e-03

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: 40.59  E-value: 2.66e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 518801140 379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:COG1053    8 VVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
379-448 3.57e-03

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 40.58  E-value: 3.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518801140 379 VIGAGPAGLACAKTAAERGHHVTLFD---AQSQ-----IGGQLNIAKTVPGKqefneTLRYFAHELSQLKVDVRLNAW 448
Cdd:PTZ00052  10 VIGGGSGGMAAAKEAAAHGKKVALFDyvkPSTQgtkwgLGGTCVNVGCVPKK-----LMHYAANIGSIFHHDSQMYGW 82
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
375-402 3.69e-03

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 40.02  E-value: 3.69e-03
                         10        20
                 ....*....|....*....|....*...
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTL 402
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTL 28
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
373-475 3.77e-03

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 40.15  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 373 NSKRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNiaktvpgkQEFNETLryfAHELSQLKVDVRLNAWADA- 451
Cdd:PRK13512 147 QVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMD--------ADMNQPI---LDELDKREIPYRLNEEIDAi 215
                         90       100       110
                 ....*....|....*....|....*....|...
gi 518801140 452 ---------AQLQDFDEIVLASGIHPRQVNIEG 475
Cdd:PRK13512 216 ngnevtfksGKVEHYDMIIEGVGTHPNSKFIES 248
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
375-463 4.55e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 39.67  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIAKTVPgkqefnetlRYfaheLSQLKVDVRLNAWADAAQ- 453
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENP---------RY----LPGIKLPDNLRATTDLAEa 68
                         90
                 ....*....|
gi 518801140 454 LQDFDEIVLA 463
Cdd:PRK00094  69 LADADLILVA 78
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
358-405 4.57e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 40.24  E-value: 4.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 518801140 358 PFACHELQLIQKPAKNskRIAVIGAGPAGLACAKTAAERGHHVTLFDA 405
Cdd:PRK08132   9 PYRPHADQDADDPARH--PVVVVGAGPVGLALAIDLAQQGVPVVLLDD 54
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
379-411 4.74e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 40.09  E-value: 4.74e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 518801140 379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQIGG 411
Cdd:PRK06134  17 VIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
375-414 4.83e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 39.96  E-value: 4.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518801140 375 KRIAVIGAGPAGLACAKTAAERGHHVTLFD-----------AQSQIGGQLN 414
Cdd:PRK08641   4 GKVIVVGGGLAGLMATIKAAEAGVHVDLFSlvpvkrshsvcAQGGINGAVN 54
PLN02576 PLN02576
protoporphyrinogen oxidase
371-413 5.01e-03

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 40.00  E-value: 5.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 518801140 371 AKNSKRIAVIGAGPAGLACA-KTAAERGHHVTLFDAQSQIGGQL 413
Cdd:PLN02576   9 AASSKDVAVVGAGVSGLAAAyALASKHGVNVLVTEARDRVGGNI 52
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
379-412 5.25e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 39.78  E-value: 5.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 518801140 379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQ--IGGQ 412
Cdd:COG3573   10 VVGAGLAGLVAAAELADAGRRVLLLDQEPEanLGGQ 45
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
374-403 5.34e-03

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 39.66  E-value: 5.34e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERGHHVTLF 403
Cdd:COG1206    1 MKPVTVIGGGLAGSEAAWQLAERGVPVRLY 30
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
369-404 5.90e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 39.71  E-value: 5.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 518801140 369 KPAKNSKRIAVIGAGPAGLACAKTAAERGHHVTLFD 404
Cdd:COG2509   25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLE 60
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
374-403 6.14e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 39.36  E-value: 6.14e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 518801140 374 SKRIAVIGAGPAGLACAKTAAERGHHVTLF 403
Cdd:PRK05335   2 MKPVNVIGAGLAGSEAAWQLAKRGVPVELY 31
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
369-404 7.53e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 37.49  E-value: 7.53e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 518801140   369 KPAKnskrIAVIGAGPAGLACAKTAAERGHHVTLFD 404
Cdd:smart01002  19 PPAK----VVVIGAGVVGLGAAATAKGLGAEVTVLD 50
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
376-422 8.50e-03

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 39.07  E-value: 8.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 518801140 376 RIAVIGAGPAGLACAKTAAERGHHVTLFDAQSqIGGQLNIAKTVPGK 422
Cdd:PRK07845   3 RIVIIGGGPGGYEAALVAAQLGADVTVIERDG-LGGAAVLTDCVPSK 48
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
379-473 9.07e-03

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 38.98  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518801140 379 VIGAGPAGLACAKTAAERGHHVTLFDAQSQIGGQLNIAKTVPGKqefneTLRYFAHELSQLK-----VDVRLNAWADAAQ 453
Cdd:PRK05249  10 VIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSK-----ALREAVLRLIGFNqnplySSYRVKLRITFAD 84
                         90       100
                 ....*....|....*....|
gi 518801140 454 LQDFDEIVLAsgihpRQVNI 473
Cdd:PRK05249  85 LLARADHVIN-----KQVEV 99
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
374-410 9.79e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 38.78  E-value: 9.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 518801140 374 SKRIAVIGAGPAGLACAK---TAAERGHHVTLFDAQSQIG 410
Cdd:COG4529    5 RKRIAIIGGGASGTALAIhllRRAPEPLRITLFEPRPELG 44
 
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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