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Conserved domains on  [gi|489214819|ref|WP_003123510|]
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MULTISPECIES: FAD-binding and (Fe-S)-binding domain-containing protein [Pseudomonas]

Protein Classification

FAD-binding and (Fe-S)-binding domain-containing protein( domain architecture ID 11416044)

FAD-binding and (Fe-S)-binding domain-containing protein, where the N-terminal FAD-binding and the C-terminal (Fe-S)-binding domains may function as oxidoreductases

Gene Ontology:  GO:0050660|GO:0046872|GO:0051536|GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
13-519 6.29e-124

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 383.86  E-value: 6.29e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  13 RLIPRERRFDDPLSTLAFGTD-ASFYRLIPKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAI--SDSVLLVL 89
Cdd:COG0277   11 RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVplDGGVVLDL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  90 GdNWNG-REIRADGAQIRLQPGVIGAQANAWLAPFGRKIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLL 168
Cdd:COG0277   91 S-RMNRiLEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 169 LADGTRLDsedpasvaafrashgellerlaeLGRETRanaelaakirhkyrlKNTTGlslnalvdYDepldiLTHLMVGS 248
Cdd:COG0277  170 LADGEVVR-----------------------TGGRVP---------------KNVTG--------YD-----LFWLLVGS 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 249 EGTLGFISAVTYDTVPEHPHKASALLVFPTVETCCTAVAVLKRQ--PVSAVELLDRRSLRSVENMQGM--PEwvkslsAG 324
Cdd:COG0277  199 EGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAgiAPAALELMDRAALALVEAAPPLglPE------DG 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 325 ACALLIESRAASRTLLHEQLGRIMAsIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRetGTTVIIEDVTFPVER 404
Cdd:COG0277  273 GALLLVEFDGDDAEEVEAQLARLRA-ILEAGGATDVRVAADGAERERLWKARKAALPALGRLD--GGAKLLEDVAVPPSR 349

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 405 LAEGVNRLIELFDKHRYdEAILFGHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLVaVEYGGSLKAEHGTGRNMAPF 484
Cdd:COG0277  350 LPELLRELGALAAKYGL-RATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLV-AELGGSISGEHGIGRLKAEF 427

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 489214819 485 VELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDD 519
Cdd:COG0277  428 LPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 463-929 2.34e-77

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


:

Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 258.85  E-value: 2.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 463 VAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDDPQSHLKNLKPLP--AADEIVDKC 540
Cdd:COG0247    1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLHDKNLKTLPwkELLDALDAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 541 IECGFCEPVCPSRGLT----LTPRQRIVLWRDIqakkRAGVDTTALERDYrYQGIDTCAATGLCAQRCPVNINTGELIRK 616
Cdd:COG0247   81 VGCGFCRAMCPSYKATgdekDSPRGRINLLREV----LEGELPLDLSEEV-YEVLDLCLTCKACETACPSGVDIADLIAE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 617 LRGAdarhaegatwlarnfagamraarfallaadgarrllgapllarasrglsQASGGRVPQWTPALPQPVRLAPPTapl 696
Cdd:COG0247  156 ARAQ-------------------------------------------------LVERGGRPLRDRLLRTFPDRVPAA--- 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 697 DDERPRVVYLAACVSRAMGPafgdeerePLLDKTRRLLEKAGYQVVFPDnlDNLCCGQPFASKGYAKQADDKRDELLAAL 776
Cdd:COG0247  184 DKEGAEVLLFPGCFTNYFDP--------EIGKAAVRLLEAAGVEVVLPP--EELCCGAPALSKGDLDLARKLARRNIEAL 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 777 LQAsrgGLDPIYCDTSPCTLRLVQGL-----DDPRLQIHDPVKFIRSHLLD-RLEFIPQDKPVAVHVTCSTQHL-GESQA 849
Cdd:COG0247  254 ERL---GVKAIVTTCPSCGLTLKDEYpellgDRVAFEVLDISEFLAELILEgKLKLKPLGEKVTYHDPCHLGRGgGVYDA 330

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 850 LIDLVGRC--TRKVVIPEGIHCCGFAGDKGFTTPELNAHSLRSLKDAVQ--FCEEGVSTSRTCEIGLS---EHGGIDYRG 922
Cdd:COG0247  331 PRELLKAIpgVEVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRatGADVVVTACPSCRTQLEdgtKEYGIEVKH 410


                 ....*..
gi 489214819 923 VVYLVDR 929
Cdd:COG0247  411 PVELLAE 417
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
13-519 6.29e-124

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 383.86  E-value: 6.29e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  13 RLIPRERRFDDPLSTLAFGTD-ASFYRLIPKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAI--SDSVLLVL 89
Cdd:COG0277   11 RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVplDGGVVLDL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  90 GdNWNG-REIRADGAQIRLQPGVIGAQANAWLAPFGRKIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLL 168
Cdd:COG0277   91 S-RMNRiLEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 169 LADGTRLDsedpasvaafrashgellerlaeLGRETRanaelaakirhkyrlKNTTGlslnalvdYDepldiLTHLMVGS 248
Cdd:COG0277  170 LADGEVVR-----------------------TGGRVP---------------KNVTG--------YD-----LFWLLVGS 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 249 EGTLGFISAVTYDTVPEHPHKASALLVFPTVETCCTAVAVLKRQ--PVSAVELLDRRSLRSVENMQGM--PEwvkslsAG 324
Cdd:COG0277  199 EGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAgiAPAALELMDRAALALVEAAPPLglPE------DG 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 325 ACALLIESRAASRTLLHEQLGRIMAsIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRetGTTVIIEDVTFPVER 404
Cdd:COG0277  273 GALLLVEFDGDDAEEVEAQLARLRA-ILEAGGATDVRVAADGAERERLWKARKAALPALGRLD--GGAKLLEDVAVPPSR 349

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 405 LAEGVNRLIELFDKHRYdEAILFGHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLVaVEYGGSLKAEHGTGRNMAPF 484
Cdd:COG0277  350 LPELLRELGALAAKYGL-RATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLV-AELGGSISGEHGIGRLKAEF 427

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 489214819 485 VELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDD 519
Cdd:COG0277  428 LPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 463-929 2.34e-77

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 258.85  E-value: 2.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 463 VAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDDPQSHLKNLKPLP--AADEIVDKC 540
Cdd:COG0247    1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLHDKNLKTLPwkELLDALDAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 541 IECGFCEPVCPSRGLT----LTPRQRIVLWRDIqakkRAGVDTTALERDYrYQGIDTCAATGLCAQRCPVNINTGELIRK 616
Cdd:COG0247   81 VGCGFCRAMCPSYKATgdekDSPRGRINLLREV----LEGELPLDLSEEV-YEVLDLCLTCKACETACPSGVDIADLIAE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 617 LRGAdarhaegatwlarnfagamraarfallaadgarrllgapllarasrglsQASGGRVPQWTPALPQPVRLAPPTapl 696
Cdd:COG0247  156 ARAQ-------------------------------------------------LVERGGRPLRDRLLRTFPDRVPAA--- 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 697 DDERPRVVYLAACVSRAMGPafgdeerePLLDKTRRLLEKAGYQVVFPDnlDNLCCGQPFASKGYAKQADDKRDELLAAL 776
Cdd:COG0247  184 DKEGAEVLLFPGCFTNYFDP--------EIGKAAVRLLEAAGVEVVLPP--EELCCGAPALSKGDLDLARKLARRNIEAL 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 777 LQAsrgGLDPIYCDTSPCTLRLVQGL-----DDPRLQIHDPVKFIRSHLLD-RLEFIPQDKPVAVHVTCSTQHL-GESQA 849
Cdd:COG0247  254 ERL---GVKAIVTTCPSCGLTLKDEYpellgDRVAFEVLDISEFLAELILEgKLKLKPLGEKVTYHDPCHLGRGgGVYDA 330

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 850 LIDLVGRC--TRKVVIPEGIHCCGFAGDKGFTTPELNAHSLRSLKDAVQ--FCEEGVSTSRTCEIGLS---EHGGIDYRG 922
Cdd:COG0247  331 PRELLKAIpgVEVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRatGADVVVTACPSCRTQLEdgtKEYGIEVKH 410


                 ....*..
gi 489214819 923 VVYLVDR 929
Cdd:COG0247  411 PVELLAE 417
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 266-515 4.73e-73

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 240.68  E-value: 4.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  266 HPHKASALLVFPTVETCCTAVAVLKRQ--PVSAVELLDRRSLRSVENMQGMPEWvkSLSAGACALLIESRAASRTLLHEQ 343
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAgiIPAALELMDNDALDLVEATLGFPKG--LPRDAAALLLVEFEGDDEETAEEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  344 LgRIMASIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRETGTTVIIEDVTFPVERLAEGVNRLIELFDKHrYDE 423
Cdd:pfam02913  80 L-EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLRDALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKY-GLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  424 AILFGHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLvAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRL 503
Cdd:pfam02913 158 VCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDL-ALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAA 236

                         250
                  ....*....|..
gi 489214819  504 LDPRGILNPGVV 515
Cdd:pfam02913 237 FDPKGILNPGKV 248
glcD TIGR00387
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ...
 48-513 3.24e-57

glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]


Pssm-ID: 273050 [Multi-domain]  Cd Length: 413  Bit Score: 202.70  E-value: 3.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819   48 ESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAI--SDSVLLVLGDNWNGREIRADGAQIRLQPGVIGAQANAWLAPFGR 125
Cdd:TIGR00387   5 KNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALpeEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVEEHNL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  126 KIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLLLADGtrldsedpasvaafrashgellERLAELGREtr 205
Cdd:TIGR00387  85 FYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADG----------------------EILRIGGKT-- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  206 anaelaakirhkyrLKNTTGlslnalvdYDepldiLTHLMVGSEGTLGFISAVTYDTVPEHPHKASALLVFPTVETCCTA 285
Cdd:TIGR00387 141 --------------AKDVAG--------YD-----LTGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFFDSIEKAMQA 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  286 VAVLKRQPV--SAVELLDRRSLRSVENM--QGMPEwvkslSAGAcALLIEsraasRTLLHEQLGRIMASIAEYPLE---K 358
Cdd:TIGR00387 194 VYDIIAAGIipAGMEFLDNLSIKAVEDIsgIGLPK-----DAGA-ILLVE-----IDGVHEAVERDEEKIEQICRKngaV 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  359 QVDFSEDPAVYNQLWRIRKDTFPAVGAVretGTTVIIEDVTFPVERLAEGVNRLIELFDKHrYDEAILFGHALEGNLHFV 438
Cdd:TIGR00387 263 DVQIAQDEEERALLWAGRRNAFKAASKL---SPLYLIEDGTVPRSKLPEALRGIADIASKY-DFTIANFGHAGDGNLHPT 338

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489214819  439 FTQGFDSPEQIARYSAFMDDVAHLvAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPRGILNPG 513
Cdd:TIGR00387 339 ILTDPEDKGEMERVEEAGGEIFEL-AIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIKKAFDPDNILNPG 412
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 35-513 1.86e-36

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 144.92  E-value: 1.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  35 SFYRLIPKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQA--ISDSVLLVLGDNWNGREIRADGAQIRLQPGVI 112
Cdd:PRK11230  50 SAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGAlpLEKGVLLVMARFNRILDINPVGRRARVQPGVR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 113 GAQANAWLAPFGRKIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLLLADGTRLdsedpasvaafrashge 192
Cdd:PRK11230 130 NLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEAL----------------- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 193 llerlaELGRETranaelaakirhkyrlknttglslnalvdYDEPLDILTHLMVGSEGTLGFISAVTYDTVPEhPHKASA 272
Cdd:PRK11230 193 ------TLGSDA-----------------------------LDSPGFDLLALFTGSEGMLGVVTEVTVKLLPK-PPVARV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 273 LLV-FPTVETCCTAVAVLKRQPV--SAVELLDRRSLRSVENM--QGMPewvkslsAGACALLIESRAASRTLLHEQLGRI 347
Cdd:PRK11230 237 LLAsFDSVEKAGLAVGDIIAAGIipGGLEMMDNLSIRAAEDFihAGYP-------VDAEAILLCELDGVESDVQEDCERV 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 348 mASIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRETGTTViieDVTFPVERLAEGVNRLIELFDKHRYDEAILF 427
Cdd:PRK11230 310 -NDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCM---DGTIPRRELPGVLEGIARLSQQYGLRVANVF 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 428 gHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLvAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPR 507
Cdd:PRK11230 386 -HAGDGNMHPLILFDANEPGELERAEALGGKILEL-CVEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPD 463


                 ....*.
gi 489214819 508 GILNPG 513
Cdd:PRK11230 464 GLLNPG 469
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
533-878 2.70e-10

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 63.35  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 533 ADEIVDKCIECGFCEPVCP-SRGLTLTPRQRIV---LWRdIQAKKRAGVDttalerdyryQGIDTCAATGLCAQRCPVNI 608
Cdd:PRK11168   2 SDTSFDSCIKCTVCTTACPvARVNPLYPGPKQAgpdGER-LRLKDGALYD----------ESLKYCSNCKRCEVACPSGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 609 NTGELIRKLRGA-DARHAEG---------------ATWLAR--NFAGAMRAarfallaadgARRLLGAPLLARASRGLSQ 670
Cdd:PRK11168  71 KIGDIIQRARAKyVTERGPPlrdrilshtdlmgslATPFAPlvNAATGLKP----------VRWLLEKTLGIDHRRPLPK 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 671 ASGGRVPQWtpalpqpvrLAPPTAPLDDERPRVVYLAACVSRAMGPAFGDEereplldkTRRLLEKAGYQVVFPDNLdnl 750
Cdd:PRK11168 141 YAFGTFRRW---------YRKQAAQQAQYKKQVAYFHGCYVNYNHPQLGKD--------LVKVLNAMGYEVLLPKEK--- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 751 CCGQPFASKGYAKQADDKRDELLAALLQASRGGLdPIYCDTSPCTLRLVQ------GLDDPRL--QIHDPVKFIRSHLLD 822
Cdd:PRK11168 201 CCGLPLIANGFLDKARKQAEFNVESLREAIEKGI-PVIATSSSCTLTLRDeypellGVDNAGVrdHIEDATEFLRRLLDQ 279

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489214819 823 R--LEFIPQDKPVAVHVTCstqHLgESQAL----IDLVGRCTRKVVIPEGIHCCGFAGDKGF 878
Cdd:PRK11168 280 GklLPLKPLPLKVAYHTPC---HL-EKQGWglytLELLRLIPGLEVVVLDSQCCGIAGTYGF 337
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 539-609 2.21e-09

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 54.39  E-value: 2.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489214819  539 KCIECGFCEPVCPSRGLTLTPRQRIVlwRDIQAKKragvdttaLERDYRYQGIDTCAATGLCAQRCPVNIN 609
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDEPKKLM--RAAYLGD--------LEELQANKVANLCSECGLCEYACPMGLD 61
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 534-607 2.04e-05

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 44.71  E-value: 2.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489214819  534 DEIVDKCIECGFCEPVCPSRGLtltprqRIVLWRDIQAKKRAgvdttalerdYRYQgID--TCAATGLCAQRCPVN 607
Cdd:TIGR01971  39 PNGEEKCIGCTLCAAVCPADAI------RVVPAEGEDGKRRL----------KFYE-INfgRCIFCGLCEEACPTD 97
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 538-607 1.95e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 42.00  E-value: 1.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPRQRIVlwrdiqakkragVDTtalerdyryqgiDTCAATGLCAQRCPVN 607
Cdd:cd10549   78 EKCIGCGLCVKVCPVDAITLEDELEIV------------IDK------------EKCIGCGICAEVCPVN 123
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
13-519 6.29e-124

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 383.86  E-value: 6.29e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  13 RLIPRERRFDDPLSTLAFGTD-ASFYRLIPKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAI--SDSVLLVL 89
Cdd:COG0277   11 RAILAGRVLTDPADRAAYARDgNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVplDGGVVLDL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  90 GdNWNG-REIRADGAQIRLQPGVIGAQANAWLAPFGRKIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLL 168
Cdd:COG0277   91 S-RMNRiLEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 169 LADGTRLDsedpasvaafrashgellerlaeLGRETRanaelaakirhkyrlKNTTGlslnalvdYDepldiLTHLMVGS 248
Cdd:COG0277  170 LADGEVVR-----------------------TGGRVP---------------KNVTG--------YD-----LFWLLVGS 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 249 EGTLGFISAVTYDTVPEHPHKASALLVFPTVETCCTAVAVLKRQ--PVSAVELLDRRSLRSVENMQGM--PEwvkslsAG 324
Cdd:COG0277  199 EGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAgiAPAALELMDRAALALVEAAPPLglPE------DG 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 325 ACALLIESRAASRTLLHEQLGRIMAsIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRetGTTVIIEDVTFPVER 404
Cdd:COG0277  273 GALLLVEFDGDDAEEVEAQLARLRA-ILEAGGATDVRVAADGAERERLWKARKAALPALGRLD--GGAKLLEDVAVPPSR 349

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 405 LAEGVNRLIELFDKHRYdEAILFGHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLVaVEYGGSLKAEHGTGRNMAPF 484
Cdd:COG0277  350 LPELLRELGALAAKYGL-RATAFGHAGDGNLHVRILFDPADPEEVERARAAAEEIFDLV-AELGGSISGEHGIGRLKAEF 427

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 489214819 485 VELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDD 519
Cdd:COG0277  428 LPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 463-929 2.34e-77

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 258.85  E-value: 2.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 463 VAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDDPQSHLKNLKPLP--AADEIVDKC 540
Cdd:COG0247    1 LSGGHGGGLKAEHGTGRFMAPFLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLHDKNLKTLPwkELLDALDAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 541 IECGFCEPVCPSRGLT----LTPRQRIVLWRDIqakkRAGVDTTALERDYrYQGIDTCAATGLCAQRCPVNINTGELIRK 616
Cdd:COG0247   81 VGCGFCRAMCPSYKATgdekDSPRGRINLLREV----LEGELPLDLSEEV-YEVLDLCLTCKACETACPSGVDIADLIAE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 617 LRGAdarhaegatwlarnfagamraarfallaadgarrllgapllarasrglsQASGGRVPQWTPALPQPVRLAPPTapl 696
Cdd:COG0247  156 ARAQ-------------------------------------------------LVERGGRPLRDRLLRTFPDRVPAA--- 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 697 DDERPRVVYLAACVSRAMGPafgdeerePLLDKTRRLLEKAGYQVVFPDnlDNLCCGQPFASKGYAKQADDKRDELLAAL 776
Cdd:COG0247  184 DKEGAEVLLFPGCFTNYFDP--------EIGKAAVRLLEAAGVEVVLPP--EELCCGAPALSKGDLDLARKLARRNIEAL 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 777 LQAsrgGLDPIYCDTSPCTLRLVQGL-----DDPRLQIHDPVKFIRSHLLD-RLEFIPQDKPVAVHVTCSTQHL-GESQA 849
Cdd:COG0247  254 ERL---GVKAIVTTCPSCGLTLKDEYpellgDRVAFEVLDISEFLAELILEgKLKLKPLGEKVTYHDPCHLGRGgGVYDA 330

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 850 LIDLVGRC--TRKVVIPEGIHCCGFAGDKGFTTPELNAHSLRSLKDAVQ--FCEEGVSTSRTCEIGLS---EHGGIDYRG 922
Cdd:COG0247  331 PRELLKAIpgVEVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRatGADVVVTACPSCRTQLEdgtKEYGIEVKH 410


                 ....*..
gi 489214819 923 VVYLVDR 929
Cdd:COG0247  411 PVELLAE 417
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 266-515 4.73e-73

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 240.68  E-value: 4.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  266 HPHKASALLVFPTVETCCTAVAVLKRQ--PVSAVELLDRRSLRSVENMQGMPEWvkSLSAGACALLIESRAASRTLLHEQ 343
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAgiIPAALELMDNDALDLVEATLGFPKG--LPRDAAALLLVEFEGDDEETAEEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  344 LgRIMASIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRETGTTVIIEDVTFPVERLAEGVNRLIELFDKHrYDE 423
Cdd:pfam02913  80 L-EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLRDALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKY-GLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  424 AILFGHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLvAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRL 503
Cdd:pfam02913 158 VCLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDL-ALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAA 236

                         250
                  ....*....|..
gi 489214819  504 LDPRGILNPGVV 515
Cdd:pfam02913 237 FDPKGILNPGKV 248
glcD TIGR00387
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ...
 48-513 3.24e-57

glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]


Pssm-ID: 273050 [Multi-domain]  Cd Length: 413  Bit Score: 202.70  E-value: 3.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819   48 ESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAI--SDSVLLVLGDNWNGREIRADGAQIRLQPGVIGAQANAWLAPFGR 125
Cdd:TIGR00387   5 KNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALpeEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVEEHNL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  126 KIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLLLADGtrldsedpasvaafrashgellERLAELGREtr 205
Cdd:TIGR00387  85 FYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADG----------------------EILRIGGKT-- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  206 anaelaakirhkyrLKNTTGlslnalvdYDepldiLTHLMVGSEGTLGFISAVTYDTVPEHPHKASALLVFPTVETCCTA 285
Cdd:TIGR00387 141 --------------AKDVAG--------YD-----LTGLFVGSEGTLGIVTEATLKLLPKPENIVVALAFFDSIEKAMQA 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  286 VAVLKRQPV--SAVELLDRRSLRSVENM--QGMPEwvkslSAGAcALLIEsraasRTLLHEQLGRIMASIAEYPLE---K 358
Cdd:TIGR00387 194 VYDIIAAGIipAGMEFLDNLSIKAVEDIsgIGLPK-----DAGA-ILLVE-----IDGVHEAVERDEEKIEQICRKngaV 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  359 QVDFSEDPAVYNQLWRIRKDTFPAVGAVretGTTVIIEDVTFPVERLAEGVNRLIELFDKHrYDEAILFGHALEGNLHFV 438
Cdd:TIGR00387 263 DVQIAQDEEERALLWAGRRNAFKAASKL---SPLYLIEDGTVPRSKLPEALRGIADIASKY-DFTIANFGHAGDGNLHPT 338

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489214819  439 FTQGFDSPEQIARYSAFMDDVAHLvAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPRGILNPG 513
Cdd:TIGR00387 339 ILTDPEDKGEMERVEEAGGEIFEL-AIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIKKAFDPDNILNPG 412
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 41-176 1.67e-36

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 134.25  E-value: 1.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819   41 PKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAISDSVLLVLGDNWNG-REIRADGAQIRLQPGVIGAQANAW 119
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRLNGiLEIDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489214819  120 LAPFGRKIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLLLADGTRLD 176
Cdd:pfam01565  81 LAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 35-513 1.86e-36

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 144.92  E-value: 1.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  35 SFYRLIPKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQA--ISDSVLLVLGDNWNGREIRADGAQIRLQPGVI 112
Cdd:PRK11230  50 SAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGAlpLEKGVLLVMARFNRILDINPVGRRARVQPGVR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 113 GAQANAWLAPFGRKIGPDPASINACKIGGIVANNASGMCCGTAQNSYHTLAGLRLLLADGTRLdsedpasvaafrashge 192
Cdd:PRK11230 130 NLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEAL----------------- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 193 llerlaELGRETranaelaakirhkyrlknttglslnalvdYDEPLDILTHLMVGSEGTLGFISAVTYDTVPEhPHKASA 272
Cdd:PRK11230 193 ------TLGSDA-----------------------------LDSPGFDLLALFTGSEGMLGVVTEVTVKLLPK-PPVARV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 273 LLV-FPTVETCCTAVAVLKRQPV--SAVELLDRRSLRSVENM--QGMPewvkslsAGACALLIESRAASRTLLHEQLGRI 347
Cdd:PRK11230 237 LLAsFDSVEKAGLAVGDIIAAGIipGGLEMMDNLSIRAAEDFihAGYP-------VDAEAILLCELDGVESDVQEDCERV 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 348 mASIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVRETGTTViieDVTFPVERLAEGVNRLIELFDKHRYDEAILF 427
Cdd:PRK11230 310 -NDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCM---DGTIPRRELPGVLEGIARLSQQYGLRVANVF 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 428 gHALEGNLHFVFTQGFDSPEQIARYSAFMDDVAHLvAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPR 507
Cdd:PRK11230 386 -HAGDGNMHPLILFDANEPGELERAEALGGKILEL-CVEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPD 463


                 ....*.
gi 489214819 508 GILNPG 513
Cdd:PRK11230 464 GLLNPG 469
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 35-513 6.56e-33

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 135.14  E-value: 6.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  35 SFYRL--IPKLVLRVESEDEVAAILSAAYREQVPVTFRAAGTSLSGQAIS--DSVLLVLGDNWNGREIRADGAQIRLQPG 110
Cdd:PLN02805 126 SFHKAvnIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAphGGVCIDMSLMKSVKALHVEDMDVVVEPG 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 111 VIGAQANAWLAPFGRKIGPDPASinACKIGGIVANNASGMCC---GTAQNSyhtLAGLRLLLADGtrlDSEDPASVAafr 187
Cdd:PLN02805 206 IGWLELNEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAvryGTMRDN---VISLKVVLPNG---DVVKTASRA--- 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 188 ashgellerlaelgRETRANaelaakirhkyrlknttglslnalvdYDepldiLTHLMVGSEGTLGFISAVTY--DTVPE 265
Cdd:PLN02805 275 --------------RKSAAG--------------------------YD-----LTRLVIGSEGTLGVITEVTLrlQKIPQ 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 266 HphKASALLVFPTVETCC-TAVA-VLKRQPVSAVELLDRRSLRSVE--NMQGMPEwvkslsagACALLIE---SRAASRt 338
Cdd:PLN02805 310 H--SVVAMCNFPTIKDAAdVAIAtMLSGIQVSRVELLDEVQIRAINmaNGKNLPE--------APTLMFEfigTEAYAR- 378

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 339 llhEQlGRIMASIAEYPLEKQVDFSEDPAVYNQLWRIRKDTFPAVGAVrETGTTVIIEDVTFPVERLAEGVNRLIELFDK 418
Cdd:PLN02805 379 ---EQ-TLIVQKIASKHNGSDFVFAEEPEAKKELWKIRKEALWACFAM-EPKYEAMITDVCVPLSHLAELISRSKKELDA 453

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 419 HRYdEAILFGHALEGNLHFV--FTQGFDSPEQIA-RYSAFMDDVAhlvaVEYGGSLKAEHGTGRNMAPFVELEWGEDAYR 495
Cdd:PLN02805 454 SPL-VCTVIAHAGDGNFHTIilFDPSQEDQRREAeRLNHFMVHTA----LSMEGTCTGEHGVGTGKMKYLEKELGIEALQ 528

                        490
                 ....*....|....*...
gi 489214819 496 LMWQLKRLLDPRGILNPG 513
Cdd:PLN02805 529 TMKRIKKALDPNNIMNPG 546
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
533-878 2.70e-10

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 63.35  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 533 ADEIVDKCIECGFCEPVCP-SRGLTLTPRQRIV---LWRdIQAKKRAGVDttalerdyryQGIDTCAATGLCAQRCPVNI 608
Cdd:PRK11168   2 SDTSFDSCIKCTVCTTACPvARVNPLYPGPKQAgpdGER-LRLKDGALYD----------ESLKYCSNCKRCEVACPSGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 609 NTGELIRKLRGA-DARHAEG---------------ATWLAR--NFAGAMRAarfallaadgARRLLGAPLLARASRGLSQ 670
Cdd:PRK11168  71 KIGDIIQRARAKyVTERGPPlrdrilshtdlmgslATPFAPlvNAATGLKP----------VRWLLEKTLGIDHRRPLPK 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 671 ASGGRVPQWtpalpqpvrLAPPTAPLDDERPRVVYLAACVSRAMGPAFGDEereplldkTRRLLEKAGYQVVFPDNLdnl 750
Cdd:PRK11168 141 YAFGTFRRW---------YRKQAAQQAQYKKQVAYFHGCYVNYNHPQLGKD--------LVKVLNAMGYEVLLPKEK--- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 751 CCGQPFASKGYAKQADDKRDELLAALLQASRGGLdPIYCDTSPCTLRLVQ------GLDDPRL--QIHDPVKFIRSHLLD 822
Cdd:PRK11168 201 CCGLPLIANGFLDKARKQAEFNVESLREAIEKGI-PVIATSSSCTLTLRDeypellGVDNAGVrdHIEDATEFLRRLLDQ 279

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489214819 823 R--LEFIPQDKPVAVHVTCstqHLgESQAL----IDLVGRCTRKVVIPEGIHCCGFAGDKGF 878
Cdd:PRK11168 280 GklLPLKPLPLKVAYHTPC---HL-EKQGWglytLELLRLIPGLEVVVLDSQCCGIAGTYGF 337
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 539-609 2.21e-09

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 54.39  E-value: 2.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489214819  539 KCIECGFCEPVCPSRGLTLTPRQRIVlwRDIQAKKragvdttaLERDYRYQGIDTCAATGLCAQRCPVNIN 609
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDEPKKLM--RAAYLGD--------LEELQANKVANLCSECGLCEYACPMGLD 61
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
537-618 4.47e-09

Heterodisulfide reductase, subunit C [Energy production and conversion];


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 53.75  E-value: 4.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 537 VDKCIECGFCEPVCPSRGLT-LTPRQRIvlwRDIQAKKRagvdttalERDYRYQGIDTCAATGLCAQRCPVNINTGELIR 615
Cdd:COG1150    2 LKKCYQCGTCTASCPVARAMdYNPRKII---RLAQLGLK--------EEVLKSDSIWLCVSCYTCTERCPRGIDIADVMD 70


                 ...
gi 489214819 616 KLR 618
Cdd:COG1150   71 ALR 73
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 539-608 6.39e-09

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 53.08  E-value: 6.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489214819  539 KCIECGFCEPVCPS-RGLTLTPRQRIvlwrdiqAKKRAGVDTTALERDYRYQGIDTCAATGLCAQRCPVNI 608
Cdd:pfam13183   1 RCIRCGACLAACPVyLVTGGRFPGDP-------RGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 540-608 7.69e-07

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 46.75  E-value: 7.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489214819  540 CIECGFCEPVCPSRGLTLTPRQrivlwrDIQAKKRAGVDttalerdyryqgIDTCAATGLCAQRCPVNI 608
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVG------EKKGTKTVVID------------PERCVGCGACVAVCPTGA 51
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 534-607 2.04e-05

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 44.71  E-value: 2.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489214819  534 DEIVDKCIECGFCEPVCPSRGLtltprqRIVLWRDIQAKKRAgvdttalerdYRYQgID--TCAATGLCAQRCPVN 607
Cdd:TIGR01971  39 PNGEEKCIGCTLCAAVCPADAI------RVVPAEGEDGKRRL----------KFYE-INfgRCIFCGLCEEACPTD 97
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 540-618 3.41e-05

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 46.27  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  540 CIECGFCEPVCPSRGLT--------LTPRQRIVL-WRDIQAKKRagvdttaLERDYRYQGIDTCAATGLCAQRCPVNINT 610
Cdd:TIGR00384 140 CILCGCCYSSCPAFWWNpeflgpaaLTAAYRFLIdSRDHATKDR-------LEGLNDKNGVWRCTTCMNCSEVCPKGVNP 212


                  ....*...
gi 489214819  611 GELIRKLR 618
Cdd:TIGR00384 213 ARAIEKLK 220
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 538-607 1.95e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 42.00  E-value: 1.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPRQRIVlwrdiqakkragVDTtalerdyryqgiDTCAATGLCAQRCPVN 607
Cdd:cd10549   78 EKCIGCGLCVKVCPVDAITLEDELEIV------------IDK------------EKCIGCGICAEVCPVN 123
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 538-607 2.62e-04

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 40.42  E-value: 2.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489214819 538 DKCIECGFCEPVCPsrgltltprqrivlwrdiqakkragvDTTALERDYRYQGIDT--CAATGLCAQRCPVN 607
Cdd:COG1144   30 DKCIGCGLCWIVCP--------------------------DGAIRVDDGKYYGIDYdyCKGCGICAEVCPVK 75
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 538-608 3.97e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 41.23  E-value: 3.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPRQRIVLWRDIqakkragvdttalerDYryqgiDTCAATGLCAQRCPVNI 608
Cdd:cd10549    6 EKCIGCGICVKACPTDAIELGPNGAIARGPEI---------------DE-----DKCVFCGACVEVCPTGA 56
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 524-776 4.00e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 43.84  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 524 LKNLKPLPAadeivdkCIECGFCEPVCPSRGLTLTP-----RQRIVLWRDiqakKRagvDTTALERDYRYQGIDTCAATG 598
Cdd:PRK06259 126 IEDIKKLRG-------CIECLSCVSTCPARKVSDYPgptfmRQLARFAFD----PR---DEGDREKEAFDEGLYNCTTCG 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 599 LCAQRCPVNINT-GELIRKLRgadarhaegatwlARNFagamraarfallaadgaRRLLGAPlLARASRGLSQASGGRVP 677
Cdd:PRK06259 192 KCVEVCPKEIDIpGKAIEKLR-------------ALAF-----------------KKGLGLP-AHLEVRENVLKTGRSVP 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 678 QWTPALpqpVRLAPPTAPLDDERPRVVYLAACVSRAMGPAFGDEereplldkTRRLLEKAGYQVVFPDNldNLCCGQPFA 757
Cdd:PRK06259 241 KEKPSF---LEEVSDIYPYGNEKLRVAFFTGCLVDYRLQEVGKD--------AIRVLNAHGISVIIPKN--QVCCGSPLI 307

                        250
                 ....*....|....*....
gi 489214819 758 SKGYAKQADDKRDELLAAL 776
Cdd:PRK06259 308 RTGQTDVAEELKKKNLEIF 326
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 511-608 1.18e-03

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 42.78  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 511 NPGVVLSD---------------DPQShlKNLKPLPAADEIVD---KCIECGFCEPVCPsrgltltPRQRIVlwrDIQAK 572
Cdd:cd01916  322 IPGVLILDpekvgevavevamavKPKR--KGEKKLPTDEEFQElaaKCTDCGWCTRACP-------NSLRIK---EAMEA 389

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489214819 573 KRAGvDTTALERDYryqgiDTCAATGLCAQRCPVNI 608
Cdd:cd01916  390 AKEG-DFSGLADLF-----DQCVGCGRCEQECPKEI 419
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 538-607 1.44e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 39.69  E-value: 1.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPRqrivLWRDIQAKKRAGVDttalerdyryqgIDTCAATGLCAQRCPVN 607
Cdd:cd10549   40 DKCVFCGACVEVCPTGAIELTPE----GKEYVPKEKEAEID------------EEKCIGCGLCVKVCPVD 93
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 538-607 1.48e-03

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 37.80  E-value: 1.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPRQRIVLWRdiqakkragVDTtalerdyryqgiDTCAATGLCAQRCPVN 607
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDGEPGKVYV---------IDP------------DKCIGCGLCVEVCPTG 50
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 538-568 1.94e-03

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 37.42  E-value: 1.94e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPRQRIVLWRD 568
Cdd:COG1143   35 DKCIGCGLCVEVCPTGAISMTPFELAVEDRE 65
NapF COG1145
Ferredoxin [Energy production and conversion];
366-607 2.29e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 40.86  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 366 PAVYNQLWRIRKDTFPAVGAVRETGTTVIIEDVTFPVERLAEGVNRLIELFDKHRYDEAILFGHALEGNLHFVFTQGFDS 445
Cdd:COG1145    8 KEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIVRVGIA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 446 PEQIARYSAFMD-DVAHLVAVEYGGSLKAEHGTGRNMAPFVELEWGEDAYRLMWQLKRLLDPRGILNPGVVLSDDPQSHL 524
Cdd:COG1145   88 AADLNLKAVALVlLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 525 KNLKPLPAADEIV-DKCIECGFCEPVCPSRGLTLTPRQRIVLwrdiqakkragVDTtalerdyryqgiDTCAATGLCAQR 603
Cdd:COG1145  168 LKIAIKKAKAVIDaEKCIGCGLCVKVCPTGAIRLKDGKPQIV-----------VDP------------DKCIGCGACVKV 224


                 ....
gi 489214819 604 CPVN 607
Cdd:COG1145  225 CPVG 228
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
539-560 3.76e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.09  E-value: 3.76e-03
                         10        20
                 ....*....|....*....|..
gi 489214819 539 KCIECGFCEPVCPSRGLTLTPR 560
Cdd:PRK05888  98 RCIFCGFCEEACPTDAIVETPD 119
NapF COG1145
Ferredoxin [Energy production and conversion];
523-561 6.44e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 39.32  E-value: 6.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489214819 523 HLKNLKPLPAADEivDKCIECGFCEPVCPSRGLTLTPRQ 561
Cdd:COG1145  200 RLKDGKPQIVVDP--DKCIGCGACVKVCPVGAISLEPKE 236
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 538-560 6.77e-03

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 36.24  E-value: 6.77e-03
                         10        20
                 ....*....|....*....|...
gi 489214819 538 DKCIECGFCEPVCPSRGLTLTPR 560
Cdd:COG1149   41 DLCTGCGACVGVCPTGAITLEER 63
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 703-794 8.75e-03

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 36.14  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819  703 VVYLAACvsramgpAFGDEEREPLLDKTRRLLEKAGYQVVFPDnlDNLCCGQPFASKGYAKQADDKRDELLAALLQAsrg 782
Cdd:pfam02754   1 VAYFDGC-------HLGRALYPEPRKALKKVLGALGVEVVILE--KQSCCGAGGGFSGKEDVAEALAKRNIDTAEET--- 68

                          90
                  ....*....|..
gi 489214819  783 GLDPIycdTSPC 794
Cdd:pfam02754  69 GADAI---VTAC 77
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 539-624 9.04e-03

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


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 38.96  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489214819 539 KCIECGFCEPVCPSRGLTLT---P------RQRIVLWRDIQAKKRAGvdttALERDYryqGIDTCAATGLCAQRCPVNIN 609
Cdd:COG0479  143 ECILCGACVAACPNVWANPDflgPaalaqaYRFALDPRDEETEERLE----ALEDEE---GVWRCTTCGNCTEVCPKGIP 215

                         90
                 ....*....|....*
gi 489214819 610 TGELIRKLRGADARH 624
Cdd:COG0479  216 PTKAIAKLKREALKR 230
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
540-607 9.70e-03

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 35.54  E-value: 9.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489214819  540 CIECGFCEPVCPSRGLTLTPR----QRIVLWRDIQAKKragvDTTALERDYRYQGIDTCaatGLCAQRCPVN 607
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGvldaRRCISYLTIEKKG----LIPDELRCLLGNRCYGC---DICQDVCPWN 65
 
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.
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