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Conserved domains on  [gi|492734902|ref|WP_005939782|]
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NAD(P)/FAD-dependent oxidoreductase [Faecalibacterium prausnitzii]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 14292863)

NAD(P)/FAD-dependent oxidoreductase with a (2Fe-2S)-binding domain 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
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-404 8.35e-133

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


:

Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 390.28  E-value: 8.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRY-KLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAE 79
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  80 ELNFPFKRCGKVLVGNTPEDMEQLERTMKQGAVNGCTGLEMIDEAKLHELVPAVV--GKFAMWSKNSGIMDPFLYTVALA 157
Cdd:COG0579   81 ELGIPFKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 158 ENAHANGVDFFFDHKVEAITRENERYYLHTAHGDFCTRWVVNAAGLGAKQISDLLGL-TDYRVIGSRSNYIILHKRMgKL 236
Cdd:COG0579  161 ENAEANGVELLLNTEVTGIEREGDGWEVTTNGGTIRARFVINAAGLYADRLAQMAGIgKDFGIFPVKGEYLVLDKPA-EL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 237 LPMPVYPVPSNTY--MGIHITPTVDGNVTVGPDAENTDVLDDY---------------------------SVPQANMDSL 287
Cdd:COG0579  240 VNAKVYPVPDPGApfLGVHLTRTIDGNLLFGPNAVFVPKKEDSlldlfeslrfpnfwpmlaknlltkyleSVTSLSKEAF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 288 AVEGAKLWPHIFKKDQIRTFAGIQPKWVDENGaiqDWKVEIRDDvaPNAVNLVGIESPGLTGSVPLARYVIGLMQEREKF 367
Cdd:COG0579  320 LEALRKYVPELPDEDLIPAFAGIRAQIIKPDG---DFVIEEADD--PGSIHVLGIESPGATSALAIAEHVAELLPEKLEE 394

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 492734902 368 eenPDFDPHHKGIvKFAEctpeqqaelIAQDPDYGEM 404
Cdd:COG0579  395 ---KDWQPKRKMI-SFGE---------LKEDPAYGEI 418
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 403-452 4.48e-17

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: 74.88  E-value: 4.48e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 492734902 403 EMICSCEEVTKAEILQAIHNPLgVSTMTGIKYRTRAMMGGCQGGFCQMKI 452
Cdd:cd19946    1 TIVCRCEEVTEGEIRDAIRRGA-ARDLDGLKRRTRAGMGRCQGRFCAPRV 49
 
Name Accession Description Interval E-value
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-404 8.35e-133

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 390.28  E-value: 8.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRY-KLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAE 79
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  80 ELNFPFKRCGKVLVGNTPEDMEQLERTMKQGAVNGCTGLEMIDEAKLHELVPAVV--GKFAMWSKNSGIMDPFLYTVALA 157
Cdd:COG0579   81 ELGIPFKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 158 ENAHANGVDFFFDHKVEAITRENERYYLHTAHGDFCTRWVVNAAGLGAKQISDLLGL-TDYRVIGSRSNYIILHKRMgKL 236
Cdd:COG0579  161 ENAEANGVELLLNTEVTGIEREGDGWEVTTNGGTIRARFVINAAGLYADRLAQMAGIgKDFGIFPVKGEYLVLDKPA-EL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 237 LPMPVYPVPSNTY--MGIHITPTVDGNVTVGPDAENTDVLDDY---------------------------SVPQANMDSL 287
Cdd:COG0579  240 VNAKVYPVPDPGApfLGVHLTRTIDGNLLFGPNAVFVPKKEDSlldlfeslrfpnfwpmlaknlltkyleSVTSLSKEAF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 288 AVEGAKLWPHIFKKDQIRTFAGIQPKWVDENGaiqDWKVEIRDDvaPNAVNLVGIESPGLTGSVPLARYVIGLMQEREKF 367
Cdd:COG0579  320 LEALRKYVPELPDEDLIPAFAGIRAQIIKPDG---DFVIEEADD--PGSIHVLGIESPGATSALAIAEHVAELLPEKLEE 394

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 492734902 368 eenPDFDPHHKGIvKFAEctpeqqaelIAQDPDYGEM 404
Cdd:COG0579  395 ---KDWQPKRKMI-SFGE---------LKEDPAYGEI 418
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 6-357 1.88e-62

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: 206.87  E-value: 1.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902    6 DVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAEELN--F 83
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALDLWEELEEELGidC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   84 PFKRCGKVLVGnTPEDMEQLERTMKQGAVNGCtGLEMIDEAKLHELVPAVVG-KFAMWSKNSGIMDPFLYTVALAENAHA 162
Cdd:pfam01266  81 GFRRCGVLVLA-RDEEEEALEKLLAALRRLGV-PAELLDAEELRELEPLLPGlRGGLFYPDGGHVDPARLLRALARAAEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  163 NGVDFFFDHKVEAITRENERYYLHTAHGdfcTRWVVNAAGLGAKQIsdLLGLTDYRVIGSRSNYIILHKRMGKLLPMPVy 242
Cdd:pfam01266 159 LGVRIIEGTEVTGIEEEGGVWGVVTTGE---ADAVVNAAGAWADLL--ALPGLRLPVRPVRGQVLVLEPLPEALLILPV- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  243 PVPSNTYMGIHITPTVDGNVTVGPDAENTDVlDDYSVPQANMDSLAVEGAKLWPHIfkKDQIRTFAGIQPKwVDENGAiq 322
Cdd:pfam01266 233 PITVDPGRGVYLRPRADGRLLLGGTDEEDGF-DDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLRPL-PDGLPI-- 306

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 492734902  323 dwkveIRDDVAPNAVNLVGIESPGLTGSVPLARYV 357
Cdd:pfam01266 307 -----IGRPGSPGLYLATGHGGHGLTLAPGIGKLL 336
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
5-358 7.63e-56

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 190.80  E-value: 7.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   5 YDVVIIGAGVVGSAIAREL-SRY-KLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAEELN 82
Cdd:PRK11728   3 YDFVIIGGGIVGLSTAMQLqERYpGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQHG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  83 FPFKRCGKVLVGNTPEDMEQLERTMKQGAVNGCTgLEMIDEAKLHELVPAVVGKFAMWSKNSGIMDPFLYTVALAENAHA 162
Cdd:PRK11728  83 IPYEECGKLLVATSELELERMEALYERARANGIE-VERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELIQA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 163 NGVDFFFDHKVEAITRENERYYLHTAHGDFCTRWVVNAAGLGAKQISDLLGL-TDYRVIGSRSNYIILHKRMGKLLPMPV 241
Cdd:PRK11728 162 RGGEIRLGAEVTALDEHANGVVVRTTQGEYEARTLINCAGLMSDRLAKMAGLePDFRIVPFRGEYYRLAPEKNQLVNHLI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 242 YPVPSNTY--MGIHITPTVDGNVTVGPDA------EN--------TDVLDDYSVP------QANMDSLAVEGA------- 292
Cdd:PRK11728 242 YPVPDPAFpfLGVHLTRMIDGSVTVGPNAvlafkrEGyrkrdfslRDLLEILTYPgfwklaQKHWRSGLGEMKnslsksg 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492734902 293 ------KLWPHIFKKDQIRTFAGIQPKWVDENGaiqdwkvEIRDD----VAPNAVNLVGIESPGLTGSVPLARYVI 358
Cdd:PRK11728 322 ylrlvqKYCPSLTLSDLQPYPAGVRAQAVSRDG-------KLVDDflfvETPRSLHVCNAPSPAATSSLPIGEHIV 390
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 403-452 4.48e-17

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: 74.88  E-value: 4.48e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 492734902 403 EMICSCEEVTKAEILQAIHNPLgVSTMTGIKYRTRAMMGGCQGGFCQMKI 452
Cdd:cd19946    1 TIVCRCEEVTEGEIRDAIRRGA-ARDLDGLKRRTRAGMGRCQGRFCAPRV 49
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
 404-458 1.21e-07

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: 47.91  E-value: 1.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 492734902  404 MICSCEEVTKAEILQAIHNplGVSTMTGIKYRTRAMMgGCQGgfCQMKIEHFIEQ 458
Cdd:pfam04324   1 IVCRCFGVTDGEIRDAIRE--GLTTVEEVKRRTKAGT-GCGS--CRPAIEEILAE 50
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 375-463 1.48e-05

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 47.52  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  375 PHHKGIVKFAECTPEQQAELIAQDPDyGEMICSCEEVTKAEILQAIHNPlGVSTMTGIKYRTRAmMGGCQGgfCQMKIEH 454
Cdd:TIGR02374 383 SEDPAIIKPQISGPEAGGPGVEAMPD-SEQICSCNTVTKGAIIDAIHTG-SCTTVEELKACTKA-GTSCGG--CKPLVEQ 457


                  ....*....
gi 492734902  455 FIEQELGTE 463
Cdd:TIGR02374 458 LLRAELNSQ 466
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-35 2.73e-03

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: 39.61  E-value: 2.73e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 492734902    5 YDVVIIGAGVVGSAIARELSRYKLSIAVLEK 35
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEK 31
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
404-461 2.77e-03

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


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 35.95  E-value: 2.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492734902 404 MICSCEEVTKAEILQAIHNplGVSTMTGIKYRTRAmMGGCqgGFCQMKIEHFIEQELG 461
Cdd:COG2906    2 YVCLCNGVTDRQIRAAIAE--GATSLEELRAALGA-GTQC--GSCVPEARELLAEALA 54
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 405-472 8.05e-03

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 38.95  E-value: 8.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492734902 405 ICSCEEVTKAEILQAIHNplGVSTMTGIKYRTRAMMgGCQGgfCQMKIEHFIEQEL---GTEP-----ENVRYSRQ 472
Cdd:PRK14989 424 ICSCFDVTKGDLIAAINK--GCHTVAALKAETKAGT-GCGG--CIPLVTQVLNAELakqGIEVnnnlcEHFAYSRQ 494
 
Name Accession Description Interval E-value
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-404 8.35e-133

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 390.28  E-value: 8.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRY-KLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAE 79
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  80 ELNFPFKRCGKVLVGNTPEDMEQLERTMKQGAVNGCTGLEMIDEAKLHELVPAVV--GKFAMWSKNSGIMDPFLYTVALA 157
Cdd:COG0579   81 ELGIPFKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 158 ENAHANGVDFFFDHKVEAITRENERYYLHTAHGDFCTRWVVNAAGLGAKQISDLLGL-TDYRVIGSRSNYIILHKRMgKL 236
Cdd:COG0579  161 ENAEANGVELLLNTEVTGIEREGDGWEVTTNGGTIRARFVINAAGLYADRLAQMAGIgKDFGIFPVKGEYLVLDKPA-EL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 237 LPMPVYPVPSNTY--MGIHITPTVDGNVTVGPDAENTDVLDDY---------------------------SVPQANMDSL 287
Cdd:COG0579  240 VNAKVYPVPDPGApfLGVHLTRTIDGNLLFGPNAVFVPKKEDSlldlfeslrfpnfwpmlaknlltkyleSVTSLSKEAF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 288 AVEGAKLWPHIFKKDQIRTFAGIQPKWVDENGaiqDWKVEIRDDvaPNAVNLVGIESPGLTGSVPLARYVIGLMQEREKF 367
Cdd:COG0579  320 LEALRKYVPELPDEDLIPAFAGIRAQIIKPDG---DFVIEEADD--PGSIHVLGIESPGATSALAIAEHVAELLPEKLEE 394

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 492734902 368 eenPDFDPHHKGIvKFAEctpeqqaelIAQDPDYGEM 404
Cdd:COG0579  395 ---KDWQPKRKMI-SFGE---------LKEDPAYGEI 418
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 6-357 1.88e-62

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: 206.87  E-value: 1.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902    6 DVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAEELN--F 83
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALDLWEELEEELGidC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   84 PFKRCGKVLVGnTPEDMEQLERTMKQGAVNGCtGLEMIDEAKLHELVPAVVG-KFAMWSKNSGIMDPFLYTVALAENAHA 162
Cdd:pfam01266  81 GFRRCGVLVLA-RDEEEEALEKLLAALRRLGV-PAELLDAEELRELEPLLPGlRGGLFYPDGGHVDPARLLRALARAAEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  163 NGVDFFFDHKVEAITRENERYYLHTAHGdfcTRWVVNAAGLGAKQIsdLLGLTDYRVIGSRSNYIILHKRMGKLLPMPVy 242
Cdd:pfam01266 159 LGVRIIEGTEVTGIEEEGGVWGVVTTGE---ADAVVNAAGAWADLL--ALPGLRLPVRPVRGQVLVLEPLPEALLILPV- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  243 PVPSNTYMGIHITPTVDGNVTVGPDAENTDVlDDYSVPQANMDSLAVEGAKLWPHIfkKDQIRTFAGIQPKwVDENGAiq 322
Cdd:pfam01266 233 PITVDPGRGVYLRPRADGRLLLGGTDEEDGF-DDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLRPL-PDGLPI-- 306

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 492734902  323 dwkveIRDDVAPNAVNLVGIESPGLTGSVPLARYV 357
Cdd:pfam01266 307 -----IGRPGSPGLYLATGHGGHGLTLAPGIGKLL 336
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
5-358 7.63e-56

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 190.80  E-value: 7.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   5 YDVVIIGAGVVGSAIAREL-SRY-KLSIAVLEKNLDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAEELN 82
Cdd:PRK11728   3 YDFVIIGGGIVGLSTAMQLqERYpGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQHG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  83 FPFKRCGKVLVGNTPEDMEQLERTMKQGAVNGCTgLEMIDEAKLHELVPAVVGKFAMWSKNSGIMDPFLYTVALAENAHA 162
Cdd:PRK11728  83 IPYEECGKLLVATSELELERMEALYERARANGIE-VERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELIQA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 163 NGVDFFFDHKVEAITRENERYYLHTAHGDFCTRWVVNAAGLGAKQISDLLGL-TDYRVIGSRSNYIILHKRMGKLLPMPV 241
Cdd:PRK11728 162 RGGEIRLGAEVTALDEHANGVVVRTTQGEYEARTLINCAGLMSDRLAKMAGLePDFRIVPFRGEYYRLAPEKNQLVNHLI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 242 YPVPSNTY--MGIHITPTVDGNVTVGPDA------EN--------TDVLDDYSVP------QANMDSLAVEGA------- 292
Cdd:PRK11728 242 YPVPDPAFpfLGVHLTRMIDGSVTVGPNAvlafkrEGyrkrdfslRDLLEILTYPgfwklaQKHWRSGLGEMKnslsksg 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492734902 293 ------KLWPHIFKKDQIRTFAGIQPKWVDENGaiqdwkvEIRDD----VAPNAVNLVGIESPGLTGSVPLARYVI 358
Cdd:PRK11728 322 ylrlvqKYCPSLTLSDLQPYPAGVRAQAVSRDG-------KLVDDflfvETPRSLHVCNAPSPAATSSLPIGEHIV 390
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
3-310 1.59e-48

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 170.86  E-value: 1.59e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   3 KQYDVVIIGAGVVGSAIARELSRYKLSIAVLEKNlDVCNETSGRNSAVVHGGFANPIGSLKAKCCVEGNKIMGQLAEELN 82
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGSGASGRNAGQLRPGLAALADRALVRLAREALDLWRELAAELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  83 --FPFKRCGKVLVGNTPEDMEQLERTMKQGAVNGCTgLEMIDEAKLHELVPAVVG---KFAMWSKNSGIMDPFLYTVALA 157
Cdd:COG0665   80 idCDFRRTGVLYLARTEAELAALRAEAEALRALGLP-VELLDAAELREREPGLGSpdyAGGLYDPDDGHVDPAKLVRALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 158 ENAHANGVDFFFDHKVEAITRENERYY-LHTAHGDFCTRWVVNAAGLGAKQISDLLGLtDYRVIGSRSNYIILhKRMGKL 236
Cdd:COG0665  159 RAARAAGVRIREGTPVTGLEREGGRVTgVRTERGTVRADAVVLAAGAWSARLLPMLGL-RLPLRPVRGYVLVT-EPLPDL 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492734902 237 LPMPVYpvpsnTYMGIHITPTVDGNVTVGPDAENTDvlDDYSVPQANMDSLAVEGAKLWPHIFKKDQIRTFAGI 310
Cdd:COG0665  237 PLRPVL-----DDTGVYLRPTADGRLLVGGTAEPAG--FDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGL 303
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
6-448 5.25e-20

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 92.77  E-value: 5.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   6 DVVIIGAGVVGSAIARELSRYKLSIAVLEKNlDVCNETSGRNSAVVHGG--FA-NPIGSlkAKCCVEGNKIMGQLAeeln 82
Cdd:PRK11101   8 DVIIIGGGATGAGIARDCALRGLRCILVERH-DIATGATGRNHGLLHSGarYAvTDAES--ARECISENQILKRIA---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  83 fpfKRC---GKVLVGNTPEDMEQLERTMKQGAVNGCTGLEMID--EAKLHE--LVPAVVGKFAMwskNSGIMDPFLYTVA 155
Cdd:PRK11101  81 ---RHCvepTDGLFITLPEDDLAFQATFIRACEEAGIEAEAIDpqQALILEpaVNPALIGAVKV---PDGTVDPFRLTAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 156 LAENAHANGVDFFFDHKVEAITRENERYY-------LHTAHGDFCTRWVVNAAGLGAKQI---SDL----------LGLT 215
Cdd:PRK11101 155 NMLDAKEHGAQILTYHEVTGLIREGDTVCgvrvrdhLTGETQEIHAPVVVNAAGIWGQHIaeyADLrirmfpakgsLLIM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 216 DYRVigsrSNYIILHKRM---GKLLpmpvypVPSNTYMGIHITPT-VDgnvtvgpdaenTDVLDDYSVPQANMDSLAVEG 291
Cdd:PRK11101 235 DHRI----NNHVINRCRKpadADIL------VPGDTISLIGTTSTrID-----------YDQIDDNRVTAEEVDILLREG 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 292 AKLWPHIFKKDQIRTFAGIQP-KWVDENGAIQDWKVEI-------RDDV-----------------APNAVNLV----GI 342
Cdd:PRK11101 294 EKLAPVMAKTRILRAYAGVRPlVASDDDPSGRNVSRGIvlldhaeRDGLdgfititggklmtyrlmAEWATDAVcrklGN 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 343 ESPGLTGSVPLAryviGLMQEREKfeenpdfdpHHKGIVKFAecTP----------EQQAELIAQDPDYGEMICSCEEVT 412
Cdd:PRK11101 374 TRPCTTADTPLP----GSQEPAEV---------TLRKVISLP--APlrgsavyrhgDRAPAWLSEGRLDRSLVCECEAVT 438

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 492734902 413 KAEILQAIHNpLGVSTMTGIKYRTRAMMGGCQGGFC 448
Cdd:PRK11101 439 AGEVRYAVEN-LNVNNLLDLRRRTRVGMGTCQGELC 473
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 403-452 4.48e-17

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: 74.88  E-value: 4.48e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 492734902 403 EMICSCEEVTKAEILQAIHNPLgVSTMTGIKYRTRAMMGGCQGGFCQMKI 452
Cdd:cd19946    1 TIVCRCEEVTEGEIRDAIRRGA-ARDLDGLKRRTRAGMGRCQGRFCAPRV 49
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
 404-458 1.21e-07

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: 47.91  E-value: 1.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 492734902  404 MICSCEEVTKAEILQAIHNplGVSTMTGIKYRTRAMMgGCQGgfCQMKIEHFIEQ 458
Cdd:pfam04324   1 IVCRCFGVTDGEIRDAIRE--GLTTVEEVKRRTKAGT-GCGS--CRPAIEEILAE 50
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 7-53 1.56e-07

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 52.76  E-value: 1.56e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 492734902   7 VVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVCNETSGRNSAVVHG 53
Cdd:COG0569   98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVG 144
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
12-216 2.01e-06

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 49.20  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  12 AGVVGSAIARELSRYKLSIAVLEKNldvcnetsgrnsavvhggfanpigslkakccvegnkimgqlaeelNFP-FKRCGk 90
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKG---------------------------------------------SFPgDKICG- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  91 vlvgntpedmeqlertmkqGAVNGCTgLEMIDEAKLHELVPAVVGKFAMWSKNSGIMD-----PFLYTV-------ALAE 158
Cdd:COG0644   35 -------------------GGLLPRA-LEELEPLGLDEPLERPVRGARFYSPGGKSVElppgrGGGYVVdrarfdrWLAE 94

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492734902 159 NAHANGVDFFFDHKVEAITRENERYYLHTAHGD-FCTRWVVNAAGLGAKqISDLLGLTD 216
Cdd:COG0644   95 QAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGEeIRADYVVDADGARSL-LARKLGLKR 152
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 3-198 3.53e-06

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: 48.78  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   3 KQYDVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVcnETSGRNSAVVHggfanpiGSLKAkccvegnkimgqlaeeln 82
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPP--RPDGRGIALSP-------RSLEL------------------ 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  83 fpFKRCGkvlVGntpEDMEQLERTMKQGAV-NGCTGLEmideakLHELVPAVVGKFAMWSknsgIMDPFLYTvALAENAH 161
Cdd:COG0654   55 --LRRLG---LW---DRLLARGAPIRGIRVrDGSDGRV------LARFDAAETGLPAGLV----VPRADLER-ALLEAAR 115

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492734902 162 ANGVDFFFDHKVEAITRENERYYLHTAHGDFCT-RWVV 198
Cdd:COG0654  116 ALGVELRFGTEVTGLEQDADGVTVTLADGRTLRaDLVV 153
PTZ00383 PTZ00383
malate:quinone oxidoreductase; Provisional
 5-202 1.06e-05

malate:quinone oxidoreductase; Provisional


Pssm-ID: 240393 [Multi-domain]  Cd Length: 497  Bit Score: 47.81  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   5 YDVVIIGAGVVGSAIARELSRYK--LSIAVLEKNLDVCNETS-GR-NSAVVHggfanpIGSLKAKCCVEGNKIMGQLAEE 80
Cdd:PTZ00383  46 YDVVIVGGGVTGTALFYTLSKFTnlKKIALIERRSDFALVAShGKnNSQTIH------CGDIETNYTLEKARKVKRQADM 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  81 L-NFPFK-----------RCGKVLVGNTPEDMEQLERTMKQGAvNGCTGLEMIDEAKLHELVPAVV----GKFAMWSKNS 144
Cdd:PTZ00383 120 LrNYLTKlppserdsiifKMQKMVLGVGEKECEFLEKRYPVFK-ELFPSMQLLDKKEIHRVEPRVVlknnHTLREEPLAA 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492734902 145 GIMDPFLYTV---ALAE--------NAHANG--VDFFFDHKVEAITRENERYY-LHTAHGDFCTRWVVNAAG 202
Cdd:PTZ00383 199 LYVPNELTTVdyqKLSEsfvkharrDALVPGkkISINLNTEVLNIERSNDSLYkIHTNRGEIRARFVVVSAC 270
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 375-463 1.48e-05

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 47.52  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  375 PHHKGIVKFAECTPEQQAELIAQDPDyGEMICSCEEVTKAEILQAIHNPlGVSTMTGIKYRTRAmMGGCQGgfCQMKIEH 454
Cdd:TIGR02374 383 SEDPAIIKPQISGPEAGGPGVEAMPD-SEQICSCNTVTKGAIIDAIHTG-SCTTVEELKACTKA-GTSCGG--CKPLVEQ 457


                  ....*....
gi 492734902  455 FIEQELGTE 463
Cdd:TIGR02374 458 LLRAELNSQ 466
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 6-221 2.32e-05

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: 46.76  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   6 DVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVCNETSGRNSAVVH---------------GGFanpigsLKAKCCVEG 70
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALYpllskddnalsrffrAAF------LFARRFYDA 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902  71 NKIMGQlaeelNFPFKRCGKVLVGntpEDMEQLERTMKQGAVNGCTGL-EMIDEAKLHELVPAVVGKFAMWSKNSGIMDP 149
Cdd:PRK01747 336 LPAAGV-----AFDHDWCGVLQLA---WDEKSAEKIAKMLALGLPAELaRALDAEEAEELAGLPVPCGGIFYPQGGWLCP 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492734902 150 FLYTVALAENAhANGVDFFFDHKVEAITRENERYYLHTAHG-DFCTRWVVNAAGLGAKQISDLLGLTDYRVIG 221
Cdd:PRK01747 408 AELCRALLALA-GQQLTIHFGHEVARLEREDDGWQLDFAGGtLASAPVVVLANGHDAARFAQTAHLPLYSVRG 479
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 1-34 2.68e-05

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 46.74  E-value: 2.68e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRY-KLSIAVLE 34
Cdd:COG2303    1 MLEEYDYVIVGAGSAGCVLANRLSEDaGLRVLLLE 35
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 7-53 4.95e-05

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 42.51  E-value: 4.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 492734902    7 VVIIGAGVVGSAIARELSRYKlSIAVLEKNLDVCNETSGRNSAVVHG 53
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKDEERVEELREEGVPVVVG 46
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 5-54 2.27e-04

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 43.80  E-value: 2.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 492734902   5 YDVVIIGAGVVGSAIARELSRYKLSIAVLEKNlDVCNETSGRNSAVVHGG 54
Cdd:PRK13369   7 YDLFVIGGGINGAGIARDAAGRGLKVLLCEKD-DLAQGTSSRSGKLVHGG 55
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
9-55 2.46e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 39.44  E-value: 2.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 492734902    9 IIGAGVVGSAIARELSRYKLSIAVLEKNldvcNETSGRNSAVVHGGF 55
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKR----DRLGGNAYSYRVPGY 43
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-39 3.88e-04

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: 42.54  E-value: 3.88e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDV 39
Cdd:COG2072    3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDV 41
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 3-35 4.44e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 42.47  E-value: 4.44e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 492734902   3 KQYDVVIIGAGVVGSAIARELSRYKLSIAVLEK 35
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK 34
trkA PRK09496
Trk system potassium transporter TrkA;
2-53 6.31e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 42.03  E-value: 6.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492734902   2 KKQYDVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVCNETSGR--NSAVVHG 53
Cdd:PRK09496 229 KPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEElpNTLVLHG 282
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 3-35 1.59e-03

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: 40.84  E-value: 1.59e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 492734902   3 KQYDVVIIGAGVVGSAIARELSRYKLSIAVLEK 35
Cdd:COG1249    2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK 34
PRK11445 PRK11445
FAD-binding protein;
5-64 1.68e-03

FAD-binding protein;


Pssm-ID: 183139 [Multi-domain]  Cd Length: 351  Bit Score: 40.43  E-value: 1.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   5 YDVVIIGAGVVGSAIARELSRyKLSIAVLEKNlDVCNETsgrnsavvhgGFANPIGSLKA 64
Cdd:PRK11445   2 YDVAIIGLGPAGSALARLLAG-KMKVIAIDKK-HQCGTE----------GFSKPCGGLLA 49
PRK09126 PRK09126
FAD-dependent hydroxylase;
5-35 2.04e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 40.31  E-value: 2.04e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 492734902   5 YDVVIIGAGVVGSAIARELSRYKLSIAVLEK 35
Cdd:PRK09126   4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
3-34 2.22e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 40.29  E-value: 2.22e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 492734902   3 KQYDVVIIGAGVVGSAIARELSRYKLSIAVLE 34
Cdd:COG1231    6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLE 37
sdhA PRK06069
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
1-52 2.30e-03

succinate dehydrogenase/fumarate reductase flavoprotein subunit;


Pssm-ID: 235689 [Multi-domain]  Cd Length: 577  Bit Score: 40.43  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902   1 MKKQYDVVIIGAGVVG--SAI-ARELSRYKLSIAVLEK-----NLDVCNEtsGRNSAVVH 52
Cdd:PRK06069   2 EVLKYDVVIVGSGLAGlrAAVaAAERSGGKLSVAVVSKtqpmrSHSVSAE--GGTAAVLY 59
PRK00711 PRK00711
D-amino acid dehydrogenase;
148-244 2.37e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 40.17  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492734902 148 DPFLYTVALAENAHANGVDFFFDHKVEAITRENERYY-LHTAHGDFCTRWVVNAAGlgakqisdllgltdyrvIGSRSny 226
Cdd:PRK00711 199 DCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITgVQTGGGVITADAYVVALG-----------------SYSTA-- 259

                         90
                 ....*....|....*...
gi 492734902 227 iiLHKRMGklLPMPVYPV 244
Cdd:PRK00711 260 --LLKPLG--VDIPVYPL 273
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-35 2.73e-03

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: 39.61  E-value: 2.73e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 492734902    5 YDVVIIGAGVVGSAIARELSRYKLSIAVLEK 35
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEK 31
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
404-461 2.77e-03

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


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 35.95  E-value: 2.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492734902 404 MICSCEEVTKAEILQAIHNplGVSTMTGIKYRTRAmMGGCqgGFCQMKIEHFIEQELG 461
Cdd:COG2906    2 YVCLCNGVTDRQIRAAIAE--GATSLEELRAALGA-GTQC--GSCVPEARELLAEALA 54
NirB_Fer2_BFD-like_1 cd19943
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ...
 405-445 2.88e-03

first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large and a small subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) 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: 381076 [Multi-domain]  Cd Length: 53  Bit Score: 35.67  E-value: 2.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 492734902 405 ICSCEEVTKAEILQAIhNPLGVSTMTGIKYRTRAMM--GGCQG 445
Cdd:cd19943    6 VCGCNGVSKGAIVQAI-QEKGLTTLDEVKACTKASTscGGCTP 47
trkA PRK09496
Trk system potassium transporter TrkA;
1-58 3.32e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 39.72  E-value: 3.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492734902   1 MKkqydVVIIGAGVVGSAIARELSRYKLSIAVLEKNLDVCNETSGR-NSAVVHGGFANP 58
Cdd:PRK09496   1 MK----IIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRlDVRTVVGNGSSP 55
PRK07364 PRK07364
FAD-dependent hydroxylase;
4-34 4.30e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 39.23  E-value: 4.30e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 492734902   4 QYDVVIIGAGVVGSAIARELSRYKLSIAVLE 34
Cdd:PRK07364  18 TYDVAIVGGGIVGLTLAAALKDSGLRIALIE 48
Fer2_BFD-like cd19942
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ...
 405-445 4.43e-03

[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain 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. 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. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.


Pssm-ID: 381075 [Multi-domain]  Cd Length: 49  Bit Score: 35.11  E-value: 4.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 492734902 405 ICSCEEVTKAEILQAIHNpLGVSTMTGIkYRTRAMMGGCQG 445
Cdd:cd19942    3 VCECFAVTEKELREAIRK-GGLKTVEEL-LTGTGAGGGCGV 41
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-37 5.54e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 39.03  E-value: 5.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRYKLSIAVLEKNL 37
Cdd:PRK06370   2 PAQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGL 38
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
 5-54 5.95e-03

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 39.38  E-value: 5.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 492734902   5 YDVVIIGAGVVGSAIARELSRYKLSIAVLEKNlDVCNETSGRNSAVVHGG 54
Cdd:PLN02464  72 LDVLVVGGGATGAGVALDAATRGLRVGLVERE-DFSSGTSSRSTKLIHGG 120
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 405-472 8.05e-03

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 38.95  E-value: 8.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492734902 405 ICSCEEVTKAEILQAIHNplGVSTMTGIKYRTRAMMgGCQGgfCQMKIEHFIEQEL---GTEP-----ENVRYSRQ 472
Cdd:PRK14989 424 ICSCFDVTKGDLIAAINK--GCHTVAALKAETKAGT-GCGG--CIPLVTQVLNAELakqGIEVnnnlcEHFAYSRQ 494
PRK08013 PRK08013
oxidoreductase; Provisional
 5-36 8.48e-03

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 38.49  E-value: 8.48e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 492734902   5 YDVVIIGAGVVGSAIARELSRYKLSIAVLEKN 36
Cdd:PRK08013   4 VDVVIAGGGMVGLAVACGLQGSGLRVAVLEQR 35
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
 1-54 9.08e-03

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 38.59  E-value: 9.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492734902   1 MKKQYDVVIIGAGVVGSAIARELSRYKLSIAVLEKNlDVCNETSGRNSAVVHGG 54
Cdd:PRK12266   3 MMETYDLLVIGGGINGAGIARDAAGRGLSVLLCEQD-DLASATSSASTKLIHGG 55
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 2-35 9.38e-03

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 38.43  E-value: 9.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 492734902   2 KKQYDVVIIGAGVVGSAIARELSRYKLSIAVLEK 35
Cdd:PRK08020   3 NQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEH 36
 
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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