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Conserved domains on  [gi|1183591690|emb|SMG18273|]
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Thioredoxin reductase [Paraburkholderia susongensis]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 14289850)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-333 3.05e-30

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 119.45  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDEnPLPGGQIYR-----NVGRSPLPdaallgddyTDGADLVARF-AQARvRY 80
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATtkeieNYPGFPEG---------ISGPELAERLrEQAE-RF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 WPDTLvwqITRALEISFTRRN---GTAASGQIRAKAVVIANGAYERPCPAPGWTLP---GVMGVGAAQTllkssAALPDG 154
Cdd:COG0492    71 GAEIL---LEEVTSVDKDDGPfrvTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDG-----FFFRGK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 155 PVVLAGSGPL-----MYL--FAwqliqadRAPAAIL---DTTPSRNYWRALAQLPgalrtpaylakgrrllnairrsGVP 224
Cdd:COG0492   143 DVVVVGGGDSaleeaLYLtkFA-------SKVTLIHrrdELRASKILVERLRANP----------------------KIE 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 225 HIRQVTRFSVEGDGRAESVQY--TAKGQESRITASVVLLHQGVVPNVQLTRSIGCEhrWDEAQlcwHPRTDAWGETTVPN 302
Cdd:COG0492   194 VLWNTEVTEIEGDGRVEGVTLknVKTGEEKELEVDGVFVAIGLKPNTELLKGLGLE--LDEDG---YIVVDEDMETSVPG 268

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1183591690 303 LFVAGD--GGGIHGAIAAQTAGALTALTVSHRL 333
Cdd:COG0492   269 VFAAGDvrDYKYRQAATAAGEGAIAALSAARYL 301
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 379-432 3.21e-19

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


:

Pssm-ID: 381079 [Multi-domain]  Cd Length: 55  Bit Score: 81.05  E-value: 3.21e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183591690 379 TIVCRCEEVSAGEIR-AMARLGCTGPNQSKSFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:cd19946     1 TIVCRCEEVTEGEIRdAIRRGAARDLDGLKRRTRAGMGRCQGRFCAPRVAELLAR 55
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-333 3.05e-30

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 119.45  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDEnPLPGGQIYR-----NVGRSPLPdaallgddyTDGADLVARF-AQARvRY 80
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATtkeieNYPGFPEG---------ISGPELAERLrEQAE-RF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 WPDTLvwqITRALEISFTRRN---GTAASGQIRAKAVVIANGAYERPCPAPGWTLP---GVMGVGAAQTllkssAALPDG 154
Cdd:COG0492    71 GAEIL---LEEVTSVDKDDGPfrvTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDG-----FFFRGK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 155 PVVLAGSGPL-----MYL--FAwqliqadRAPAAIL---DTTPSRNYWRALAQLPgalrtpaylakgrrllnairrsGVP 224
Cdd:COG0492   143 DVVVVGGGDSaleeaLYLtkFA-------SKVTLIHrrdELRASKILVERLRANP----------------------KIE 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 225 HIRQVTRFSVEGDGRAESVQY--TAKGQESRITASVVLLHQGVVPNVQLTRSIGCEhrWDEAQlcwHPRTDAWGETTVPN 302
Cdd:COG0492   194 VLWNTEVTEIEGDGRVEGVTLknVKTGEEKELEVDGVFVAIGLKPNTELLKGLGLE--LDEDG---YIVVDEDMETSVPG 268

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1183591690 303 LFVAGD--GGGIHGAIAAQTAGALTALTVSHRL 333
Cdd:COG0492   269 VFAAGDvrDYKYRQAATAAGEGAIAALSAARYL 301
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 379-432 3.21e-19

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381079 [Multi-domain]  Cd Length: 55  Bit Score: 81.05  E-value: 3.21e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183591690 379 TIVCRCEEVSAGEIR-AMARLGCTGPNQSKSFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:cd19946     1 TIVCRCEEVTEGEIRdAIRRGAARDLDGLKRRTRAGMGRCQGRFCAPRVAELLAR 55
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-322 1.44e-18

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: 86.22  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDV-LVLDENPLPGGQI-----YRNVGRsPLPDAALLGDDYTDGADLVARFaQARVRY 80
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVtLIEDEGTCPYGGCvlskaLLGAAE-APEIASLWADLYKRKEEVVKKL-NNGIEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 WPDTLVWQITRAlEISFTRRNGTAASGQ-IRAKAVVIANGAYERPCPAPGWTLPGVMGVGAAQTLLKSSAALPDGPVVLA 159
Cdd:pfam07992  80 LLGTEVVSIDPG-AKKVVLEELVDGDGEtITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 160 GSGPLMYLFAWQLIQAdRAPAAILDTTPsrnywRALAQLPGALRtpaylakgRRLLNAIRRSGVP--HIRQVTRFSVEGD 237
Cdd:pfam07992 159 GGGYIGVELAAALAKL-GKEVTLIEALD-----RLLRAFDEEIS--------AALEKALEKNGVEvrLGTSVKEIIGDGD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 238 GraesVQYTAKgQESRITASVVLLHQGVVPNVQLTRSIGCEHRWDEAqlcwhPRTDAWGETTVPNLFVAGDG--GGIHGA 315
Cdd:pfam07992 225 G----VEVILK-DGTEIDADLVVVAIGRRPNTELLEAAGLELDERGG-----IVVDEYLRTSVPGIYAAGDCrvGGPELA 294


                  ....*..
gi 1183591690 316 IAAQTAG 322
Cdd:pfam07992 295 QNAVAQG 301
SO_alpha_A3 pfam17806
Sarcosine oxidase A3 domain; This short domain is found in Heterotetrameric Sarcosine Oxidase ...
 381-459 4.92e-07

Sarcosine oxidase A3 domain; This short domain is found in Heterotetrameric Sarcosine Oxidase's alpha A3 domain. This domain binds to FMN in sarcosine oxidase. This domain is related to pfam04324 but lacks its iron binding cysteine residues.


Pssm-ID: 375343 [Multi-domain]  Cd Length: 87  Bit Score: 47.37  E-value: 4.92e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183591690 381 VCRCEEVSAGEIRAMARLGCTGPNQSKSFSRCGMGPCQGRLCGLTVAELLAEAHAKPVAEVGYYRIRPPIKPVTLGDLA 459
Cdd:pfam17806   6 VDFQNDVTVKDIEQAAREGFRSIEHIKRYTTAGMGPDQGKLSAVNAAAIVARLTGRTIGEVGTTTYRPPYAPVSFAALA 84
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
380-435 1.05e-06

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 45.58  E-value: 1.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1183591690 380 IVCRCEEVSAGEIRAMARLGCTGPNQSKSFSRCGmGPCqGRlCGLTVAELLAEAHA 435
Cdd:COG2906     2 YVCLCNGVTDRQIRAAIAEGATSLEELRAALGAG-TQC-GS-CVPEARELLAEALA 54
glycerol3P_GlpA TIGR03377
glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are ...
 325-432 1.24e-06

glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are the A subunit, product of the glpA gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 274552 [Multi-domain]  Cd Length: 516  Bit Score: 50.79  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 325 TALTVSHRLGALSRESRderaaplRRQLDRH--RAVRPFLDTlyrpadafrrPADDTIVCRCEEVSAGEIR-AMARLGCT 401
Cdd:TIGR03377 368 TAVKTLKKLISLPSPIA-------GSAVYRHgeRAPQVLKDN----------RLDNQVICECEMVTAGEVEyAIRELDVN 430

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1183591690 402 GPNQSKSFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:TIGR03377 431 NLVDLRRRTRLGMGTCQGEFCAYRAAGLLSR 461
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
337-432 1.30e-06

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 50.79  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 337 SRESRDE---RAAPLRRQLdRHRAVrpfldtlYR---PADAFRR--PADDTIVCRCEEVSAGEIR-AMARLGCTGPNQSK 407
Cdd:PRK11101  387 SQEPAEVtlrKVISLPAPL-RGSAV-------YRhgdRAPAWLSegRLDRSLVCECEAVTAGEVRyAVENLNVNNLLDLR 458

                          90       100
                  ....*....|....*....|....*
gi 1183591690 408 SFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:PRK11101  459 RRTRVGMGTCQGELCACRAAGLLQR 483
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 10-136 3.30e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 49.41  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGG----QI--YRnvgrspLPDaallgddytdgadlvaRFAQARVRYwpd 83
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllryGIpeFR------LPK----------------DIVDREVER--- 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  84 tlvwqiTRALEISFtRRN---GTAAS-GQIRA--KAVVIANGAYE-RPCPAPGWTLPGVM 136
Cdd:PRK11749  200 ------LLKLGVEI-RTNtevGRDITlDELRAgyDAVFIGTGAGLpRFLGIPGENLGGVY 252
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-333 3.05e-30

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 119.45  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDEnPLPGGQIYR-----NVGRSPLPdaallgddyTDGADLVARF-AQARvRY 80
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATtkeieNYPGFPEG---------ISGPELAERLrEQAE-RF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 WPDTLvwqITRALEISFTRRN---GTAASGQIRAKAVVIANGAYERPCPAPGWTLP---GVMGVGAAQTllkssAALPDG 154
Cdd:COG0492    71 GAEIL---LEEVTSVDKDDGPfrvTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDG-----FFFRGK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 155 PVVLAGSGPL-----MYL--FAwqliqadRAPAAIL---DTTPSRNYWRALAQLPgalrtpaylakgrrllnairrsGVP 224
Cdd:COG0492   143 DVVVVGGGDSaleeaLYLtkFA-------SKVTLIHrrdELRASKILVERLRANP----------------------KIE 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 225 HIRQVTRFSVEGDGRAESVQY--TAKGQESRITASVVLLHQGVVPNVQLTRSIGCEhrWDEAQlcwHPRTDAWGETTVPN 302
Cdd:COG0492   194 VLWNTEVTEIEGDGRVEGVTLknVKTGEEKELEVDGVFVAIGLKPNTELLKGLGLE--LDEDG---YIVVDEDMETSVPG 268

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1183591690 303 LFVAGD--GGGIHGAIAAQTAGALTALTVSHRL 333
Cdd:COG0492   269 VFAAGDvrDYKYRQAATAAGEGAIAALSAARYL 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 29-321 5.08e-25

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: 104.89  E-value: 5.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  29 LDVLVLDENPLPGGQIYrnvgrsPLPDaaLLGDDYTDGADLVAR----FAQARVRYWPDTLVWQITRAleisftRRNGTA 104
Cdd:COG0446     6 AEITVIEKGPHHSYQPC------GLPY--YVGGGIKDPEDLLVRtpesFERKGIDVRTGTEVTAIDPE------AKTVTL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 105 ASGQ-IRAKAVVIANGAYERPCPAPGWTLPGVMGVGAAQTLLKSSAALPDGP---VVLAGSGPLMYLFAWQLIQADRaPA 180
Cdd:COG0446    72 RDGEtLSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKgkrAVVIGGGPIGLELAEALRKRGL-KV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 181 AILDTTPsrnywRALAQLPGALrtpaylakGRRLLNAIRRSGVPHIRQVTRFSVEGDGRAEsVQYTAKGqesRITASVVL 260
Cdd:COG0446   151 TLVERAP-----RLLGVLDPEM--------AALLEEELREHGVELRLGETVVAIDGDDKVA-VTLTDGE---EIPADLVV 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183591690 261 LHQGVVPNVQLTRSIGCEHrwdeAQLCWHPrTDAWGETTVPNLFVAGDGGGIHGAIAAQTA 321
Cdd:COG0446   214 VAPGVRPNTELAKDAGLAL----GERGWIK-VDETLQTSDPDVYAAGDCAEVPHPVTGKTV 269
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 379-432 3.21e-19

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381079 [Multi-domain]  Cd Length: 55  Bit Score: 81.05  E-value: 3.21e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183591690 379 TIVCRCEEVSAGEIR-AMARLGCTGPNQSKSFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:cd19946     1 TIVCRCEEVTEGEIRdAIRRGAARDLDGLKRRTRAGMGRCQGRFCAPRVAELLAR 55
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-322 1.44e-18

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: 86.22  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDV-LVLDENPLPGGQI-----YRNVGRsPLPDAALLGDDYTDGADLVARFaQARVRY 80
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVtLIEDEGTCPYGGCvlskaLLGAAE-APEIASLWADLYKRKEEVVKKL-NNGIEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 WPDTLVWQITRAlEISFTRRNGTAASGQ-IRAKAVVIANGAYERPCPAPGWTLPGVMGVGAAQTLLKSSAALPDGPVVLA 159
Cdd:pfam07992  80 LLGTEVVSIDPG-AKKVVLEELVDGDGEtITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 160 GSGPLMYLFAWQLIQAdRAPAAILDTTPsrnywRALAQLPGALRtpaylakgRRLLNAIRRSGVP--HIRQVTRFSVEGD 237
Cdd:pfam07992 159 GGGYIGVELAAALAKL-GKEVTLIEALD-----RLLRAFDEEIS--------AALEKALEKNGVEvrLGTSVKEIIGDGD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 238 GraesVQYTAKgQESRITASVVLLHQGVVPNVQLTRSIGCEHRWDEAqlcwhPRTDAWGETTVPNLFVAGDG--GGIHGA 315
Cdd:pfam07992 225 G----VEVILK-DGTEIDADLVVVAIGRRPNTELLEAAGLELDERGG-----IVVDEYLRTSVPGIYAAGDCrvGGPELA 294


                  ....*..
gi 1183591690 316 IAAQTAG 322
Cdd:pfam07992 295 QNAVAQG 301
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
5-308 6.35e-11

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 64.01  E-value: 6.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   5 TADLVIVGAGPAGMACA--LDAERAGLDVLVLDENPlpggqiYRNVGRSPLPDaALLGDDYTDGADLVAR--FAQARVRY 80
Cdd:COG1251     1 KMRIVIIGAGMAGVRAAeeLRKLDPDGEITVIGAEP------HPPYNRPPLSK-VLAGETDEEDLLLRPAdfYEENGIDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 WPDTLVWQITRAleisftRRNGTAASG-QIRAKAVVIANGAYERPCPAPGWTLPGVMGVGAAQTLLKSSAALPDG-PVVL 158
Cdd:COG1251    74 RLGTRVTAIDRA------ARTVTLADGeTLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGkRVVV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 159 AGSGPLMYLFAWQLIQADrAPAAILDTTPsrnywRALA-QLPGALrtpaylakGRRLLNAIRRSGVpHIR---QVTRfsV 234
Cdd:COG1251   148 IGGGLIGLEAAAALRKRG-LEVTVVERAP-----RLLPrQLDEEA--------GALLQRLLEALGV-EVRlgtGVTE--I 210

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1183591690 235 EGDGRAESVQyTAKGqeSRITASVVLLHQGVVPNVQLTRSIG--CEHRwdeaqlcwhPRTDAWGETTVPNLFVAGD 308
Cdd:COG1251   211 EGDDRVTGVR-LADG--EELPADLVVVAIGVRPNTELARAAGlaVDRG---------IVVDDYLRTSDPDIYAAGD 274
SO_alpha_A3 pfam17806
Sarcosine oxidase A3 domain; This short domain is found in Heterotetrameric Sarcosine Oxidase ...
 381-459 4.92e-07

Sarcosine oxidase A3 domain; This short domain is found in Heterotetrameric Sarcosine Oxidase's alpha A3 domain. This domain binds to FMN in sarcosine oxidase. This domain is related to pfam04324 but lacks its iron binding cysteine residues.


Pssm-ID: 375343 [Multi-domain]  Cd Length: 87  Bit Score: 47.37  E-value: 4.92e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183591690 381 VCRCEEVSAGEIRAMARLGCTGPNQSKSFSRCGMGPCQGRLCGLTVAELLAEAHAKPVAEVGYYRIRPPIKPVTLGDLA 459
Cdd:pfam17806   6 VDFQNDVTVKDIEQAAREGFRSIEHIKRYTTAGMGPDQGKLSAVNAAAIVARLTGRTIGEVGTTTYRPPYAPVSFAALA 84
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
10-73 9.60e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 45.99  E-value: 9.60e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNV---GRSPLPDAALLGDDYTDGADLVARF 73
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRvpgYVFDYGAHIFHGSDEPNVRDLLDEL 67
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
380-435 1.05e-06

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 45.58  E-value: 1.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1183591690 380 IVCRCEEVSAGEIRAMARLGCTGPNQSKSFSRCGmGPCqGRlCGLTVAELLAEAHA 435
Cdd:COG2906     2 YVCLCNGVTDRQIRAAIAEGATSLEELRAALGAG-TQC-GS-CVPEARELLAEALA 54
glycerol3P_GlpA TIGR03377
glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are ...
 325-432 1.24e-06

glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are the A subunit, product of the glpA gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 274552 [Multi-domain]  Cd Length: 516  Bit Score: 50.79  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 325 TALTVSHRLGALSRESRderaaplRRQLDRH--RAVRPFLDTlyrpadafrrPADDTIVCRCEEVSAGEIR-AMARLGCT 401
Cdd:TIGR03377 368 TAVKTLKKLISLPSPIA-------GSAVYRHgeRAPQVLKDN----------RLDNQVICECEMVTAGEVEyAIRELDVN 430

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1183591690 402 GPNQSKSFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:TIGR03377 431 NLVDLRRRTRLGMGTCQGEFCAYRAAGLLSR 461
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
337-432 1.30e-06

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 50.79  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 337 SRESRDE---RAAPLRRQLdRHRAVrpfldtlYR---PADAFRR--PADDTIVCRCEEVSAGEIR-AMARLGCTGPNQSK 407
Cdd:PRK11101  387 SQEPAEVtlrKVISLPAPL-RGSAV-------YRhgdRAPAWLSegRLDRSLVCECEAVTAGEVRyAVENLNVNNLLDLR 458

                          90       100
                  ....*....|....*....|....*
gi 1183591690 408 SFSRCGMGPCQGRLCGLTVAELLAE 432
Cdd:PRK11101  459 RRTRVGMGTCQGELCACRAAGLLQR 483
HI0933_like pfam03486
HI0933-like protein;
7-41 1.45e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 50.27  E-value: 1.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPG 41
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
 380-432 2.13e-06

BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).


Pssm-ID: 461261 [Multi-domain]  Cd Length: 50  Bit Score: 44.44  E-value: 2.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1183591690 380 IVCRCEEVSAGEIRAMARLGCTGPNQSKSFSRCGMGpCQGrlCGLTVAELLAE 432
Cdd:pfam04324   1 IVCRCFGVTDGEIRDAIREGLTTVEEVKRRTKAGTG-CGS--CRPAIEEILAE 50
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
9-41 2.20e-06

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 49.66  E-value: 2.20e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1183591690   9 VIVGAGPAGMACALDAERAGLDVLVLDENPLPG 41
Cdd:COG2081     1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 5-42 2.67e-06

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 49.85  E-value: 2.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:COG1233     3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 7-124 2.90e-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: 49.48  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNvgRSP------------LPDAALLGDD--YTDGADLVA- 71
Cdd:COG2072     8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTWRDN--RYPglrldtpshlysLPFFPNWSDDpdFPTGDEILAy 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183591690  72 --RFAQA--------------RVRYWPDTLVWQITraleisftrrngTAASGQIRAKAVVIANGAYERP 124
Cdd:COG2072    86 leAYADKfglrrpirfgtevtSARWDEADGRWTVT------------TDDGETLTARFVVVATGPLSRP 142
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 10-136 3.30e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 49.41  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGG----QI--YRnvgrspLPDaallgddytdgadlvaRFAQARVRYwpd 83
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllryGIpeFR------LPK----------------DIVDREVER--- 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  84 tlvwqiTRALEISFtRRN---GTAAS-GQIRA--KAVVIANGAYE-RPCPAPGWTLPGVM 136
Cdd:PRK11749  200 ------LLKLGVEI-RTNtevGRDITlDELRAgyDAVFIGTGAGLpRFLGIPGENLGGVY 252
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 5-42 4.70e-06

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: 48.68  E-value: 4.70e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 7-43 5.31e-06

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 48.76  E-value: 5.31e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQ 43
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-333 6.88e-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: 48.16  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLpGGqIYRNVGRSP---LPDAALLGDDYTDGADLVARFAQARVRY--- 80
Cdd:COG1249     5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL-GG-TCLNVGCIPskaLLHAAEVAHEARHAAEFGISAGAPSVDWaal 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  81 --WPDTLVWQITRALEISFTRRNGTAASG----------------QIRAKAVVIANGAyeRPcpapgWTLPgvmGVGAAQ 142
Cdd:COG1249    83 maRKDKVVDRLRGGVEELLKKNGVDVIRGrarfvdphtvevtggeTLTADHIVIATGS--RP-----RVPP---IPGLDE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 143 TLLKSS------AALPDGPVVLaGSGP----LMYLFAW---QLIQADRAPaaildttpsrnywRALAQLPGALRtpayla 209
Cdd:COG1249   153 VRVLTSdealelEELPKSLVVI-GGGYigleFAQIFARlgsEVTLVERGD-------------RLLPGEDPEIS------ 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 210 kgRRLLNAIRRSGVpHIR---QVTRFSVEGDGRaeSVQYTAKGQESRITASVVLLHQGVVPNvqlTRSIGCEH---RWDE 283
Cdd:COG1249   213 --EALEKALEKEGI-DILtgaKVTSVEKTGDGV--TVTLEDGGGEEAVEADKVLVATGRRPN---TDGLGLEAagvELDE 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1183591690 284 AQlcwHPRTDAWGETTVPNLFVAGD--GG------GIH-GAIAAQTAGALTALTVSHRL 333
Cdd:COG1249   285 RG---GIKVDEYLRTSVPGIYAIGDvtGGpqlahvASAeGRVAAENILGKKPRPVDYRA 340
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 7-41 7.52e-06

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 47.70  E-value: 7.52e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPG 41
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 2-67 7.70e-06

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 48.21  E-value: 7.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183591690   2 TIVTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNVGRSPLPDAALLGDD-----YTDGA 67
Cdd:PRK12844    3 WDETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGVLWLPNNPLMKAAgvpdsHEDAL 73
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 7-323 1.49e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 47.09  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLpGG-----------------QIYRNVGRsplpdAALLGDDYtDGADL 69
Cdd:PRK06292    5 DVIVIGAGPAGYVAARRAAKLGKKVALIEKGPL-GGtclnvgcipskaliaaaEAFHEAKH-----AEEFGIHA-DGPKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  70 VARFAQARVRYWPDTLVWQITRALE----ISFTRrnGTA---ASG-------QIRAKAVVIANGAyERPcpapgwTLPGV 135
Cdd:PRK06292   78 DFKKVMARVRRERDRFVGGVVEGLEkkpkIDKIK--GTArfvDPNtvevngeRIEAKNIVIATGS-RVP------PIPGV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 136 MgVGAAQTLLKSSAA-----LPDGPVVLaGSGPLmylfAWQLIQAdrapaaildttpsrnyWRALaqlpGALRTpaYLAK 210
Cdd:PRK06292  149 W-LILGDRLLTSDDAfeldkLPKSLAVI-GGGVI----GLELGQA----------------LSRL----GVKVT--VFER 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 211 GRRLLN----AIRRSGVPHIRQ---------VTRFSVEGDGRAESVQYTAKGQEsrITASVVLLHQGVVPNvqlTRSIGC 277
Cdd:PRK06292  201 GDRILPledpEVSKQAQKILSKefkiklgakVTSVEKSGDEKVEELEKGGKTET--IEADYVLVATGRRPN---TDGLGL 275

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1183591690 278 EH---RWDEAQlcwHPRTDAWGETTVPNLFVAGDGGGI---------HGAIAAQTAGA 323
Cdd:PRK06292  276 ENtgiELDERG---RPVVDEHTQTSVPGIYAAGDVNGKppllheaadEGRIAAENAAG 330
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
4-49 1.53e-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: 1.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1183591690   4 VTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNVG 49
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAG 46
PRK06481 PRK06481
flavocytochrome c;
7-42 1.72e-05

flavocytochrome c;


Pssm-ID: 180584 [Multi-domain]  Cd Length: 506  Bit Score: 47.14  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK06481   63 DIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGG 98
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 7-49 2.20e-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: 46.24  E-value: 2.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPG-GQIYRNVG 49
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsGASGRNAG 44
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 9-110 4.19e-05

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: 45.73  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   9 VIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYR--------NVGRSPL--PDA-----ALLGDDYTDGADLVARF 73
Cdd:TIGR02734   2 VVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVleddgfrfDTGPTVItmPEAleelfALAGRDLADYVELVPLD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1183591690  74 AQARVRyWPDTLVWQI---TRALEISFTRRNGTAASGQIR 110
Cdd:TIGR02734  82 PFYRLC-WEDGSQLDVdndQEELEAQIARFNPGDVAGYRR 120
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 1-42 5.50e-05

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 45.45  E-value: 5.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1183591690   1 MTIVTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK12842    5 TNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
PRK07190 PRK07190
FAD-binding protein;
1-51 5.88e-05

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 45.58  E-value: 5.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1183591690   1 MTIVTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPggqiyRNVGRS 51
Cdd:PRK07190    1 MSTQVTDVVIIGAGPVGLMCAYLGQLCGLNTVIVDKSDGP-----LEVGRA 46
PLN02463 PLN02463
lycopene beta cyclase
 7-39 6.11e-05

lycopene beta cyclase


Pssm-ID: 178082 [Multi-domain]  Cd Length: 447  Bit Score: 45.48  E-value: 6.11e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPL 39
Cdd:PLN02463   30 DLVVVGGGPAGLAVAQQVSEAGLSVCCIDPSPL 62
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 7-44 7.51e-05

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: 44.82  E-value: 7.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQI 44
Cdd:COG1232     3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 10-162 8.60e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 45.10  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNVGRSPLPDAALlgddYTDGADLVARFAQARVRywpdtlvwqi 89
Cdd:PRK12814  198 IIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVI----DADIAPLRAMGAEFRFN---------- 263

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183591690  90 traleisfTR--RNGTAASGQIRAKAVVIANGAYERP-CPAPGWTLPGVM-GVGAAQTLLKSSAALPDGPVVLAGSG 162
Cdd:PRK12814  264 --------TVfgRDITLEELQKEFDAVLLAVGAQKASkMGIPGEELPGVIsGIDFLRNVALGTALHPGKKVVVIGGG 332
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 7-44 9.55e-05

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: 44.59  E-value: 9.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQI 44
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
13-121 1.04e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 44.19  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690  13 AGPAGMACALDAERAGLDVLVLDENPLPGgqiYRNVGRSPLPDAALLGDDYTDGADLVARFAQARVRYWPDTLV------ 86
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGSFPG---DKICGGGLLPRALEELEPLGLDEPLERPVRGARFYSPGGKSVelppgr 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183591690  87 ---WQITRAL--------------EI-------SFTRRNG-----TAASGQIRAKAVVIANGAY 121
Cdd:COG0644    78 gggYVVDRARfdrwlaeqaeeagaEVrtgtrvtDVLRDDGrvvvrTGDGEEIRADYVVDADGAR 141
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
1-43 1.28e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 44.40  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1183591690   1 MTIVTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLP--GGQ 43
Cdd:COG3573     1 MAAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEPEAnlGGQ 45
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 10-42 1.47e-04

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: 43.97  E-value: 1.47e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:COG0493   126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 10-42 1.48e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 44.00  E-value: 1.48e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK12810  148 VVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
5-45 2.06e-04

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 43.76  E-value: 2.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIY 45
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVW 47
PRK12835 PRK12835
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 5-56 2.08e-04

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237221 [Multi-domain]  Cd Length: 584  Bit Score: 43.64  E-value: 2.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENP--------------LPGGQIYRNVGRSPLPDA 56
Cdd:PRK12835   11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAhfggstalsgggiwVPGAPAQRREGYVPDPED 76
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-73 2.24e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 43.49  E-value: 2.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183591690   1 MTIVTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNVGRSPLP-DAALLGDDYTDGADLVARF 73
Cdd:PRK07843    3 MTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGGVWIPnNEVLKRAGVPDTPEAARTY 76
PRK13984 PRK13984
putative oxidoreductase; Provisional
 10-58 2.67e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 43.60  E-value: 2.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNVGRSPLPDAAL 58
Cdd:PRK13984  288 IVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEAL 336
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
7-35 2.99e-04

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 43.18  E-value: 2.99e-04
                          10        20
                  ....*....|....*....|....*....
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLD 35
Cdd:COG2509    32 DVVIVGAGPAGLFAALELAEAGLKPLVLE 60
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 7-65 4.56e-04

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: 42.53  E-value: 4.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDE-NPLPGGQIY------RNVGRSP---LPDAALLGDDYTD 65
Cdd:TIGR01438   4 DLIVIGGGSGGLAAAKEAAAYGAKVMLLDFvTPTPLGTRWgiggtcVNVGCIPkklMHQAALLGQALKD 72
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 6-39 4.65e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 42.51  E-value: 4.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1183591690   6 ADLVIVGAGPAGMACALDAERAGLDVLVLDENPL 39
Cdd:PRK05714    3 ADLLIVGAGMVGSALALALQGSGLEVLLLDGGPL 36
PRK09126 PRK09126
FAD-dependent hydroxylase;
5-40 6.16e-04

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 41.85  E-value: 6.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLP 40
Cdd:PRK09126    3 HSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQPLA 38
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 5-41 7.41e-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: 41.46  E-value: 7.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPG 41
Cdd:COG0654     3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
gltA TIGR01316
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ...
 10-54 7.85e-04

glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130383 [Multi-domain]  Cd Length: 449  Bit Score: 41.78  E-value: 7.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGGQIYRNVGRSPLP 54
Cdd:TIGR01316 138 VIGAGPAGLACASELAKAGHSVTVFEALHKPGGVVTYGIPEFRLP 182
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 10-42 1.03e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 41.40  E-value: 1.03e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK12771  142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 2-45 1.19e-03

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


Pssm-ID: 460393  Cd Length: 232  Bit Score: 40.53  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1183591690   2 TIVTADLVIVGAGPAGMACALD-AERAGLDVLVLDENPLPGGQIY 45
Cdd:pfam01946  14 DYAESDVVIVGAGSSGLTAAYYlAKNRGLKVAIIERSVSPGGGAW 58
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
4-43 1.34e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.00  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1183591690   4 VTADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGGQ 43
Cdd:COG1148   139 VNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGR 178
PRK12845 PRK12845
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 4-72 1.40e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237226 [Multi-domain]  Cd Length: 564  Bit Score: 41.29  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183591690   4 VTADLVIVGAGpAGMACALDAERAGLDVLVLDENPLPGGQIYRNVGRSPLPDAALLGDDytDGADLVAR 72
Cdd:PRK12845   15 TTVDLLVVGSG-TGMAAALAAHELGLSVLIVEKSSYVGGSTARSGGAFWLPASPVLDEA--GAGDTLER 80
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 7-42 1.65e-03

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: 40.61  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:COG3349     5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
PRK07233 PRK07233
hypothetical protein; Provisional
 9-42 1.90e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 40.64  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1183591690   9 VIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK07233    3 AIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 9-38 1.96e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 40.62  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1183591690   9 VIVGAGPAGMACALDAERAGLDVLVLDENP 38
Cdd:PRK08132   27 VVVGAGPVGLALAIDLAQQGVPVVLLDDDD 56
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-34 1.97e-03

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 40.61  E-value: 1.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1183591690   1 MTIVTADLVIVGAGPAGMACALDAERAGLDVLVL 34
Cdd:PRK06185    2 AEVETTDCCIVGGGPAGMMLGLLLARAGVDVTVL 35
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
6-34 2.45e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 40.22  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|....*....
gi 1183591690   6 ADLVIVGAGPAGMACALDAERAGLDVLVL 34
Cdd:PRK05329    3 FDVLVIGGGLAGLTAALAAAEAGKRVALV 31
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 7-134 2.65e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 40.13  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLpGGqIYRNVGrsPLPDAALL-----------GDDYTDGADLVaRFAQ 75
Cdd:PRK06416    6 DVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKL-GG-TCLNRG--CIPSKALLhaaeradearhSEDFGIKAENV-GIDF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1183591690  76 ARVRYWPDTLVWQITRALEISFTRR-----NGTA--------------ASGQIRAKAVVIANGAYERpcpapgwTLPG 134
Cdd:PRK06416   81 KKVQEWKNGVVNRLTGGVEGLLKKNkvdiiRGEAklvdpntvrvmtedGEQTYTAKNIILATGSRPR-------ELPG 151
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 5-42 3.87e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 39.70  E-value: 3.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK06134   12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 4-45 4.35e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 39.50  E-value: 4.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1183591690   4 VTADLVIVGAGPAGMACALDAERAGLDVLVLD---ENPLpGGQIY 45
Cdd:PRK12834    3 MDADVIVVGAGLAGLVAAAELADAGKRVLLLDqenEANL-GGQAF 46
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 4-34 4.89e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.18  E-value: 4.89e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1183591690   4 VTADLVIVGAGPAGMACALDAERAGLDVLVL 34
Cdd:PRK07804   15 DAADVVVVGSGVAGLTAALAARRAGRRVLVV 45
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 10-42 5.56e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 39.34  E-value: 5.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1183591690  10 IVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK12769  332 IIGAGPAGLACADVLARNGVAVTVYDRHPEIGG 364
sdhA PRK06263
succinate dehydrogenase flavoprotein subunit; Reviewed
 291-315 6.09e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 235758 [Multi-domain]  Cd Length: 543  Bit Score: 39.19  E-value: 6.09e-03
                          10        20
                  ....*....|....*....|....*.
gi 1183591690 291 RTDAWGETTVPNLFVAGD-GGGIHGA 315
Cdd:PRK06263  352 RINEDCETNIPGLFACGEvAGGVHGA 377
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
7-42 6.44e-03

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 38.98  E-value: 6.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK05249    7 DLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 8-42 6.60e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 38.85  E-value: 6.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1183591690   8 LVIVGAGPAGMACALDAERAGLDVLVLDENPLPGG 42
Cdd:PRK12809  313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGG 347
PRK08626 PRK08626
fumarate reductase flavoprotein subunit; Provisional
 1-34 6.69e-03

fumarate reductase flavoprotein subunit; Provisional


Pssm-ID: 181507 [Multi-domain]  Cd Length: 657  Bit Score: 39.19  E-value: 6.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1183591690   1 MTIVTADLVIVGAGPAGMACALDAERAGLDVLVL 34
Cdd:PRK08626    1 MKIIYTDALVIGAGLAGLRVAIAAAQRGLDTIVL 34
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 216-313 6.95e-03

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 38.87  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 216 NAIRRSGVPHIRQVTRFSVEGDGRAESVQyTAKGqesRITASVVLLHQGVVPNVQLTRSIGCEHRWDEAQLcwhprTDAW 295
Cdd:PRK09564  199 EELRENGVELHLNEFVKSLIGEDKVEGVV-TDKG---EYEADVVIVATGVKPNTEFLEDTGLKTLKNGAII-----VDEY 269

                          90
                  ....*....|....*...
gi 1183591690 296 GETTVPNLFVAGDGGGIH 313
Cdd:PRK09564  270 GETSIENIYAAGDCATIY 287
PRK07121 PRK07121
FAD-binding protein;
5-35 7.59e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 38.71  E-value: 7.59e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLD 35
Cdd:PRK07121   20 EADVVVVGFGAAGACAAIEAAAAGARVLVLE 50
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 291-397 7.74e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 38.80  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690 291 RTDAWGETTVPNLFVAGD--GGGIHGA-----------------IAAQTAGALTALTVSHRLGALSRESRDERAAP---L 348
Cdd:PRK07804  361 VTDVYGRTSVPGLYAAGEvaCTGVHGAnrlasnslleglvvgerAGAAAAAHAAAAGRPRATPAVGPEPGLLPALDraeL 440

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1183591690 349 RRQLDRHRAVRPFLDTLYRPADAFRRPADDTIVCRCEEVSAGEIRAMAR 397
Cdd:PRK07804  441 QRAMTRGAGVLRSAAGLARAADRLAAGAPARVVPGRADWEDTNLTLVAR 489
PRK06184 PRK06184
hypothetical protein; Provisional
 5-40 8.07e-03

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 38.81  E-value: 8.07e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1183591690   5 TADLVIVGAGPAGMACALDAERAGLDVLVLDENPLP 40
Cdd:PRK06184    3 TTDVLIVGAGPTGLTLAIELARRGVSFRLIEKAPEP 38
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 7-129 8.22e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 38.60  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183591690   7 DLVIVGAGPAGMACALDAERAGLDVLVLDENplPGGQIYRNVGRSplpdaALLGDDYTDGADLVARFAQARVRYWPDTLV 86
Cdd:PRK15317  213 DVLVVGGGPAGAAAAIYAARKGIRTGIVAER--FGGQVLDTMGIE-----NFISVPETEGPKLAAALEEHVKEYDVDIMN 285

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1183591690  87 WQITRALE-----ISFTRRNGtaasGQIRAKAVVIANGAYERPCPAPG 129
Cdd:PRK15317  286 LQRASKLEpaaglIEVELANG----AVLKAKTVILATGARWRNMNVPG 329
 
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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