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Conserved domains on  [gi|1726868578|gb|TXQ73356|]
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anaerobic glycerol-3-phosphate dehydrogenase subunit C [Escherichia coli]

Protein Classification

anaerobic glycerol-3-phosphate dehydrogenase subunit C( domain architecture ID 11496778)

anaerobic glycerol-3-phosphate dehydrogenase subunit C acts as an electron transfer protein, which may also function as the membrane anchor for the GlpAB dimer

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glycerol3P_GlpC TIGR03379
glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are ...
 3-396 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species. [Energy metabolism, Anaerobic]


:

Pssm-ID: 132422 [Multi-domain]  Cd Length: 397  Bit Score: 797.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   3 DTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAK 82
Cdd:TIGR03379   1 DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKIGDIIARARNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  83 YDTTRP---SLRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQY 159
Cdd:TIGR03379  81 YQKKKPnikKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPKYSFGTFRRWYKKNATSQALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 160 KDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGVKGIPVIA 239
Cdd:TIGR03379 161 ERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIANGFPDKAKKQAQFNVKQIEAMVDENGIPVIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 240 TSSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCHMEKMGWTLYTLELLRNIPG 319
Cdd:TIGR03379 241 TSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFMEGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578 320 LELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTSLRCEHPITLLAQALA 396
Cdd:TIGR03379 321 LEVVVLDSQCCGIAGTYGFKSENYETSQAIGKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMALA 397
 
Name Accession Description Interval E-value
glycerol3P_GlpC TIGR03379
glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are ...
 3-396 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species. [Energy metabolism, Anaerobic]


Pssm-ID: 132422 [Multi-domain]  Cd Length: 397  Bit Score: 797.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   3 DTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAK 82
Cdd:TIGR03379   1 DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKIGDIIARARNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  83 YDTTRP---SLRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQY 159
Cdd:TIGR03379  81 YQKKKPnikKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPKYSFGTFRRWYKKNATSQALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 160 KDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGVKGIPVIA 239
Cdd:TIGR03379 161 ERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIANGFPDKAKKQAQFNVKQIEAMVDENGIPVIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 240 TSSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCHMEKMGWTLYTLELLRNIPG 319
Cdd:TIGR03379 241 TSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFMEGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578 320 LELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTSLRCEHPITLLAQALA 396
Cdd:TIGR03379 321 LEVVVLDSQCCGIAGTYGFKSENYETSQAIGKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMALA 397
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
1-396 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 745.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   1 MNDTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRAR 80
Cdd:PRK11168    1 MSDTSFDSCIKCTVCTTACPVARVNPLYPGPKQAGPDGERLRLKDGALYDESLKYCSNCKRCEVACPSGVKIGDIIQRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  81 AKY-DTTRPSLRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQY 159
Cdd:PRK11168   81 AKYvTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLLEKTLGIDHRRPLPKYAFGTFRRWYRKQAAQQAQY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 160 KDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVqLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGvKGIPVIA 239
Cdd:PRK11168  161 KKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEV-LLPKEKCCGLPLIANGFLDKARKQAEFNVESLREAIE-KGIPVIA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 240 TSSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCHMEKMGWTLYTLELLRNIPG 319
Cdd:PRK11168  239 TSSSCTLTLRDEYPELLGVDNAGVRDHIEDATEFLRRLLDQGKLLPLKPLPLKVAYHTPCHLEKQGWGLYTLELLRLIPG 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578 320 LELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTSLRCEHPITLLAQALA 396
Cdd:PRK11168  319 LEVVVLDSQCCGIAGTYGFKKEKYETSQAIGAPLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALG 395
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 3-396 1.64e-94

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 289.28  E-value: 1.64e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   3 DTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYD------EALKYCINCKRCEVACPSDVKIGDII 76
Cdd:COG0247    74 LDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDlseevyEVLDLCLTCKACETACPSGVDIADLI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  77 QRARAKYDTTrpslrnfvlshtdlmgsvstpfapivntatslkpvrqlldaalkidHRRTLPKYSFGTFRRWYRSVAAQQ 156
Cdd:COG0247   154 AEARAQLVER----------------------------------------------GGRPLRDRLLRTFPDRVPAADKEG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 157 AQykdqVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAvGVKGIp 236
Cdd:COG0247   188 AE----VLLFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEALERL-GVKAI- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 237 vIATSSTCTFALRDEYPEVLNVDnkgLRDHIELATRWLWRKLDEGKtLPLKPLPLKVVYHTPCHMEK-MGWTLYTLELLR 315
Cdd:COG0247   262 -VTTCPSCGLTLKDEYPELLGDR---VAFEVLDISEFLAELILEGK-LKLKPLGEKVTYHDPCHLGRgGGVYDAPRELLK 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 316 NIPGLELTVL--DSQCCGIAGTYGFKKENypTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTS---LRCEHPITL 390
Cdd:COG0247   337 AIPGVEVVEMpeDSGCCGGAGGYGFEEPE--LSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKeygIEVKHPVEL 414


                  ....*.
gi 1726868578 391 LAQALA 396
Cdd:COG0247   415 LAEALG 420
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 293-376 6.33e-17

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: 75.04  E-value: 6.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 293 VVYHTPCHMEKmGWTLYTLELLRNIPGLELTVL----DSQCCGIAGTYGFKKenyPTSQAIGAPLFRQIEESGADLVITD 368
Cdd:pfam02754   1 VAYFDGCHLGR-ALYPEPRKALKKVLGALGVEVvileKQSCCGAGGGFSGKE---DVAEALAKRNIDTAEETGADAIVTA 76


                  ....*...
gi 1726868578 369 CETCKWQI 376
Cdd:pfam02754  77 CPGCLLQL 84
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 9-83 6.33e-05

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: 45.09  E-value: 6.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578   9 CIKCTVCTTACPvsrvnPGYPGPK--QAGPDGERLRLKDgaLYDEalkyCINCKRCEVACPSDVKIGDIIQRARAKY 83
Cdd:cd01916   367 CTDCGWCTRACP-----NSLRIKEamEAAKEGDFSGLAD--LFDQ----CVGCGRCEQECPKEIPIINMIEKAARER 432
 
Name Accession Description Interval E-value
glycerol3P_GlpC TIGR03379
glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are ...
 3-396 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species. [Energy metabolism, Anaerobic]


Pssm-ID: 132422 [Multi-domain]  Cd Length: 397  Bit Score: 797.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   3 DTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAK 82
Cdd:TIGR03379   1 DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKIGDIIARARNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  83 YDTTRP---SLRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQY 159
Cdd:TIGR03379  81 YQKKKPnikKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPKYSFGTFRRWYKKNATSQALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 160 KDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGVKGIPVIA 239
Cdd:TIGR03379 161 ERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIANGFPDKAKKQAQFNVKQIEAMVDENGIPVIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 240 TSSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCHMEKMGWTLYTLELLRNIPG 319
Cdd:TIGR03379 241 TSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFMEGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578 320 LELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTSLRCEHPITLLAQALA 396
Cdd:TIGR03379 321 LEVVVLDSQCCGIAGTYGFKSENYETSQAIGKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMALA 397
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
1-396 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 745.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   1 MNDTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRAR 80
Cdd:PRK11168    1 MSDTSFDSCIKCTVCTTACPVARVNPLYPGPKQAGPDGERLRLKDGALYDESLKYCSNCKRCEVACPSGVKIGDIIQRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  81 AKY-DTTRPSLRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQY 159
Cdd:PRK11168   81 AKYvTERGPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLLEKTLGIDHRRPLPKYAFGTFRRWYRKQAAQQAQY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 160 KDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVqLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGvKGIPVIA 239
Cdd:PRK11168  161 KKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEV-LLPKEKCCGLPLIANGFLDKARKQAEFNVESLREAIE-KGIPVIA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 240 TSSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCHMEKMGWTLYTLELLRNIPG 319
Cdd:PRK11168  239 TSSSCTLTLRDEYPELLGVDNAGVRDHIEDATEFLRRLLDQGKLLPLKPLPLKVAYHTPCHLEKQGWGLYTLELLRLIPG 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578 320 LELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTSLRCEHPITLLAQALA 396
Cdd:PRK11168  319 LEVVVLDSQCCGIAGTYGFKKEKYETSQAIGAPLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALG 395
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 3-396 1.64e-94

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 289.28  E-value: 1.64e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   3 DTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYD------EALKYCINCKRCEVACPSDVKIGDII 76
Cdd:COG0247    74 LDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDlseevyEVLDLCLTCKACETACPSGVDIADLI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  77 QRARAKYDTTrpslrnfvlshtdlmgsvstpfapivntatslkpvrqlldaalkidHRRTLPKYSFGTFRRWYRSVAAQQ 156
Cdd:COG0247   154 AEARAQLVER----------------------------------------------GGRPLRDRLLRTFPDRVPAADKEG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 157 AQykdqVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAvGVKGIp 236
Cdd:COG0247   188 AE----VLLFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEALERL-GVKAI- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 237 vIATSSTCTFALRDEYPEVLNVDnkgLRDHIELATRWLWRKLDEGKtLPLKPLPLKVVYHTPCHMEK-MGWTLYTLELLR 315
Cdd:COG0247   262 -VTTCPSCGLTLKDEYPELLGDR---VAFEVLDISEFLAELILEGK-LKLKPLGEKVTYHDPCHLGRgGGVYDAPRELLK 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 316 NIPGLELTVL--DSQCCGIAGTYGFKKENypTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMSTS---LRCEHPITL 390
Cdd:COG0247   337 AIPGVEVVEMpeDSGCCGGAGGYGFEEPE--LSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKeygIEVKHPVEL 414


                  ....*.
gi 1726868578 391 LAQALA 396
Cdd:COG0247   415 LAEALG 420
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 8-395 5.31e-37

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 140.14  E-value: 5.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   8 NCIKCTVCTTACPVSRVNPgYPGP----KQA----GPDGERLRLKDGalYDEALKYCINCKRCEVACPSDVKI-GDIIQR 78
Cdd:PRK06259  134 GCIECLSCVSTCPARKVSD-YPGPtfmrQLArfafDPRDEGDREKEA--FDEGLYNCTTCGKCVEVCPKEIDIpGKAIEK 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  79 ARA---KYDTTRPS---LRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVrqlldaalkidhrrtlpkysfgtfrrwyrsv 152
Cdd:PRK06259  211 LRAlafKKGLGLPAhleVRENVLKTGRSVPKEKPSFLEEVSDIYPYGNE------------------------------- 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 153 aaqqaqyKDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREavgv 232
Cdd:PRK06259  260 -------KLRVAFFTGCLVDYRLQEVGKDAIRVLNAHGISVIIPKNQVCCGSPLIRTGQTDVAEELKKKNLEIFNK---- 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 233 KGIPVIAT-SSTCTFALRDEYPEV-LNVdnkglRDHIELatrwlwrkLDEGKTLPLKPLPLKVVYHTPCHMEK-MGWTLY 309
Cdd:PRK06259  329 LDVDTVVTiCAGCGSTLKNDYKEKeFNV-----MDITEV--------LVEVGLEKYKPLDITVTYHDPCHLRRgQGIYEE 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 310 TLELLRNIPGLELTVLD--SQCCGIAGtyGFKKENYPTSQAIGAPLFRQIEESGADLVITDCETCKWQIEMS-----TSL 382
Cdd:PRK06259  396 PRKILRSIPGLEFVEMEipDQCCGAGG--GVRSGKPEIAEALGKRKAEMIRETGADYVITVCPFCEYHIRDSlkkysEDI 473

                         410
                  ....*....|...
gi 1726868578 383 RCEHPITLLAQAL 395
Cdd:PRK06259  474 PVMNIVSLLDKVY 486
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 293-376 6.33e-17

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: 75.04  E-value: 6.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 293 VVYHTPCHMEKmGWTLYTLELLRNIPGLELTVL----DSQCCGIAGTYGFKKenyPTSQAIGAPLFRQIEESGADLVITD 368
Cdd:pfam02754   1 VAYFDGCHLGR-ALYPEPRKALKKVLGALGVEVvileKQSCCGAGGGFSGKE---DVAEALAKRNIDTAEETGADAIVTA 76


                  ....*...
gi 1726868578 369 CETCKWQI 376
Cdd:pfam02754  77 CPGCLLQL 84
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 163-248 7.33e-16

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: 71.96  E-value: 7.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 163 VAFFHGC-FVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREavgVKGIPVIATS 241
Cdd:pfam02754   1 VAYFDGChLGRALYPEPRKALKKVLGALGVEVVILEKQSCCGAGGGFSGKEDVAEALAKRNIDTAEE---TGADAIVTAC 77


                  ....*..
gi 1726868578 242 STCTFAL 248
Cdd:pfam02754  78 PGCLLQL 84
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 8-70 4.60e-11

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: 58.09  E-value: 4.60e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726868578   8 NCIKCTVCTTACPVSRVNPGYP-GPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDV 70
Cdd:pfam13183   1 RCIRCGACLAACPVYLVTGGRFpGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 6-83 1.64e-10

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: 60.53  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   6 FENCIKCTVCTTACPVSRVNPGYPGPK---QA---------GPDGERLRlkdgALYDEA-LKYCINCKRCEVACPSDVKI 72
Cdd:COG0479   141 LAECILCGACVAACPNVWANPDFLGPAalaQAyrfaldprdEETEERLE----ALEDEEgVWRCTTCGNCTEVCPKGIPP 216

                          90
                  ....*....|.
gi 1726868578  73 GDIIQRARAKY 83
Cdd:COG0479   217 TKAIAKLKREA 227
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
5-88 9.05e-10

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 58.99  E-value: 9.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   5 SFENCIKCTVCTTACPVSRVNPGYPGPkQAGPDGERLrLKD--GALYDEALKY-------CINCKRCEVACPSDVKIGDI 75
Cdd:PRK12576  150 KFAQCIWCGLCVSACPVVAIDPEFLGP-AAHAKGYRF-LADprDTITEERMKIlidsswrCTYCYSCSNVCPRDIEPVTA 227

                          90
                  ....*....|...
gi 1726868578  76 IQRARAKYDTTRP 88
Cdd:PRK12576  228 IKKTRSFTRVYKP 240
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
5-80 1.70e-09

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 54.14  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   5 SFENCIKCTVCTTACPVSRVnPGYPgPKQ----AgpdgeRLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRAR 80
Cdd:COG1150     1 NLKKCYQCGTCTASCPVARA-MDYN-PRKiirlA-----QLGLKEEVLKSDSIWLCVSCYTCTERCPRGIDIADVMDALR 73
glcF PRK11274
glycolate oxidase subunit GlcF;
8-396 3.17e-08

glycolate oxidase subunit GlcF;


Pssm-ID: 236890 [Multi-domain]  Cd Length: 407  Bit Score: 55.26  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   8 NCIKCTVCTTACPVsrvnpgYP-------GP-------KQA---GPDGERLRLKdgalydeaLKYCINCKRCEVACPSDV 70
Cdd:PRK11274   24 KCVHCGFCTATCPT------YQllgdeldGPrgriyliKQVlegAEVTEKTQLH--------LDRCLTCRNCETTCPSGV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578  71 KIGDIIQRARAKYDT----------TRPSLRNFVLShtdlmgsvSTPFAPIVNTATSLKPvrqLLDAALKidhrRTLPKy 140
Cdd:PRK11274   90 QYGRLLDIGRKVVEEkvprplgerlLRWGLREVLPR--------PALFGPLMRLGQAVRP---LLPEALR----AKVPA- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 141 sfgtfrrwyRSVAAQ--QAQYKDQVAFFHGCfV------NYNHPQlgkdlIKVLNAMGTGVQLLSKEKCCGVPLIANGFT 212
Cdd:PRK11274  154 ---------RQPAAPwpPPRHARRVLMLEGC-VqpamspNINAAT-----ARVLDRLGISLVVAPEAGCCGAVRYHLNAQ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 213 DKARKQAITNVESIREAV--GVKGIpvIATSSTCTfALRDEYPEVLNVD----NKGLRdhIELATR---WLWRKLDEGKT 283
Cdd:PRK11274  219 EGGLARMRRNIDAWWPAIeaGAEAI--VMTASGCG-ATVKEYGHLLRDDpayaEKAAR--VSALTRdlsELLPAEPLELL 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578 284 LPLKPLPLKVVYHTPC---HMEKMGWTLYTleLLRNIpGLELT-VLDSQ-CCGIAGTYGFKKenyPT-SQAIGAPLFRQI 357
Cdd:PRK11274  294 ALLGRPDRRVAFHPPCtlqHGQKLRGKVER--LLTRL-GFELTlVADSHlCCGSAGTYSLLQ---PElSYQLRDNKLAAL 367

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1726868578 358 EESGADLVITDCETCKWQIEMSTSLRCEHPITLLAQALA 396
Cdd:PRK11274  368 EAGKPEVIVTANIGCQTHLQSGTRTPVRHWIELVDEALA 406
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 6-80 2.22e-07

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: 51.28  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   6 FENCIKCTVCTTACPVSRVNPGYPGP---KQAG-------PDGERLRLKdgALYDEALKY-CINCKRCEVACPSDVKIGD 74
Cdd:TIGR00384 137 LSGCILCGCCYSSCPAFWWNPEFLGPaalTAAYrflidsrDHATKDRLE--GLNDKNGVWrCTTCMNCSEVCPKGVNPAR 214


                  ....*.
gi 1726868578  75 IIQRAR 80
Cdd:TIGR00384 215 AIEKLK 220
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 8-70 2.81e-07

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: 47.07  E-value: 2.81e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726868578   8 NCIKCTVCTTACPVSRVNPGYPgpkQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDV 70
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDEP---KKLMRAAYLGDLEELQANKVANLCSECGLCEYACPMGL 60
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 9-70 5.05e-05

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: 40.59  E-value: 5.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726868578   9 CIKCTVCTTACPVSRVNPGYPGPKQAGPDgerlrlkdgalYDEALKYCINCKRCEVACPSDV 70
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKT-----------VVIDPERCVGCGACVAVCPTGA 51
psaC CHL00065
photosystem I subunit VII
 6-69 5.39e-05

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 41.29  E-value: 5.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726868578   6 FENCIKCTVCTTACP--VSRVNPgYPGPKqAGPDGERLRLKDgalydealkyCINCKRCEVACPSD 69
Cdd:CHL00065    8 YDTCIGCTQCVRACPtdVLEMIP-WDGCK-AKQIASAPRTED----------CVGCKRCESACPTD 61
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 9-83 6.33e-05

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: 45.09  E-value: 6.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726868578   9 CIKCTVCTTACPvsrvnPGYPGPK--QAGPDGERLRLKDgaLYDEalkyCINCKRCEVACPSDVKIGDIIQRARAKY 83
Cdd:cd01916   367 CTDCGWCTRACP-----NSLRIKEamEAAKEGDFSGLAD--LFDQ----CVGCGRCEQECPKEIPIINMIEKAARER 432
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 7-82 1.30e-04

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 43.97  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   7 ENCIKCTVCTTACPVSrVNPgypgpkqagpdgerLRLKDGAL---YDEALKY----CINCKRCEVACPSDVKIGDIIQRA 79
Cdd:COG4656   364 QPCIRCGRCVDACPMG-LLP--------------QQLYWYARagdFDKAEEYnlmdCIECGCCSYVCPSKIPLVQYIRLA 428


                  ...
gi 1726868578  80 RAK 82
Cdd:COG4656   429 KAE 431
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 6-69 3.11e-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: 39.26  E-value: 3.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726868578   6 FENCIKCTVCTTACPVSrvnpgypgpkqagpdgeRLRLKDGALYDEALKYCINCKRCEVACPSD 69
Cdd:COG1144    29 EDKCIGCGLCWIVCPDG-----------------AIRVDDGKYYGIDYDYCKGCGICAEVCPVK 75
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 6-69 6.95e-04

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 38.39  E-value: 6.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726868578   6 FENCIKCTVCTTACP--VSRVNPGyPGPKqAGPDGERLRLKDgalydealkyCINCKRCEVACPSD 69
Cdd:PLN00071    8 YDTCIGCTQCVRACPtdVLEMIPW-DGCK-AKQIASAPRTED----------CVGCKRCESACPTD 61
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
8-88 1.06e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 40.83  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   8 NCIKCTVCTTACPVSRVNPGYPGPkQAGPDGERLrLKDG---------ALYDEALK---YCINCKRCEVACPSDV----K 71
Cdd:PRK12577  153 NCILCGACYSECNAREVNPEFVGP-HALAKAQRM-VADSrdtateqrlELYNQGTAgvwGCTRCYYCNSVCPMEVapldQ 230

                          90
                  ....*....|....*....
gi 1726868578  72 IGDIIQR--ARAKYDTTRP 88
Cdd:PRK12577  231 ITKIKQEilARKDAQDSRA 249
NapF COG1145
Ferredoxin [Energy production and conversion];
7-70 1.25e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 40.09  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726868578   7 ENCIKCTVCTTACPVsrvnpgypgpkQAgpdgerLRLKDG-ALYDEALKYCINCKRCEVACPSDV 70
Cdd:COG1145   182 EKCIGCGLCVKVCPT-----------GA------IRLKDGkPQIVVDPDKCIGCGACVKVCPVGA 229
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 7-69 1.61e-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: 36.65  E-value: 1.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726868578   7 ENCIKCTVCTTACPVSRVNPGYPGPKQAgpdgerlrlkdgalYDEALKYCINCKRCEVACPSD 69
Cdd:COG1143     2 DKCIGCGLCVRVCPVDAITIEDGEPGKV--------------YVIDPDKCIGCGLCVEVCPTG 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 7-70 1.88e-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: 38.15  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726868578   7 ENCIKCTVCTTACPVsrvnpgypgpkqagpdgERLRLKDGALYDEALKYCINCKRCEVACPSDV 70
Cdd:cd10549    78 EKCIGCGLCVKVCPV-----------------DAITLEDELEIVIDKEKCIGCGICAEVCPVNA 124
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 9-96 2.01e-03

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 39.59  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726868578   9 CIKCTVCTTACPVSRVNPGYPGPK--------QAGPDG-----ERLR--LKDGALYDealkyCINCKRCEVACPSDVKIG 73
Cdd:PRK08640  154 CMTCGCCLEACPNVNEKSDFIGPAaisqvrlfNAHPTGemhkeERLRalMGDGGIAD-----CGNAQNCVRVCPKGIPLT 228

                          90       100
                  ....*....|....*....|...
gi 1726868578  74 DIIqrARAKYDTTRPSLRNFVLS 96
Cdd:PRK08640  229 TSI--AAMNRETTKQSFKSFFGS 249
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 7-69 2.60e-03

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 36.23  E-value: 2.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726868578   7 ENCIKCTVCTTACPVS--RVNPGYPGPKQAGPDgerlrlkdgalydealkYCINCKRCEVACPSD 69
Cdd:COG1146     8 DKCIGCGACVEVCPVDvlELDEEGKKALVINPE-----------------ECIGCGACELVCPVG 55
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
7-70 3.18e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 38.89  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726868578   7 ENCIKCTVCTTACPVsrvnpgypgpkqagpdgeRLRLKDGALYDEAlkyCINCKRCEVACPSDV 70
Cdd:COG0348   210 GDCIDCGLCVKVCPM------------------GIDIRKGEINQSE---CINCGRCIDACPKDA 252
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 8-31 4.56e-03

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 38.24  E-value: 4.56e-03
                          10        20
                  ....*....|....*....|....*
gi 1726868578   8 NCIKCTVCTTACPVSRVNP-GYPGP 31
Cdd:PRK05950  142 ECILCACCSTSCPSFWWNPdKFLGP 166
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 7-69 5.51e-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: 35.09  E-value: 5.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726868578   7 ENCIKCTVCTTACPVsrvnpgypgpkQAgpdgerLRLKDGALYDEALKYCINCKRCEVACPSD 69
Cdd:COG1149    11 EKCIGCGLCVEVCPE-----------GA------IKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 7-78 5.77e-03

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.41  E-value: 5.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726868578   7 ENCIKCTVCTTACPVsrvnpgypgpkQAgpdgerLRLKDGALY-DEALkyCINCKRCEVACPSDVKIGDIIQR 78
Cdd:COG2221    15 EKCIGCGLCVAVCPT-----------GA------ISLDDGKLViDEEK--CIGCGACIRVCPTGAIKGEKPKK 68
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 7-70 5.79e-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: 36.61  E-value: 5.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726868578   7 ENCIKCTVCTTACPVSRVNPGYPGPKQAGPDgerlrlkdgalYDEALkyCINCKRCEVACPSDV 70
Cdd:cd10549     6 EKCIGCGICVKACPTDAIELGPNGAIARGPE-----------IDEDK--CVFCGACVEVCPTGA 56
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 9-67 6.32e-03

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: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 34.92  E-value: 6.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1726868578   9 CIKCTVCTTACPVSRVNPGYpgpKQAGPDGERLRLKDGAlydealkyCINCKRCEVACP 67
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGA---IVERLEGEAVRIGVWK--------CIGCGACVEACP 56
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 7-69 7.38e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.02  E-value: 7.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726868578   7 ENCIKCTVCTTACPVsrvnpgypgpkqagpdgERLRLKDGALY-DEALkyCINCKRCEVACPSD 69
Cdd:COG4231    22 DKCTGCGACVKVCPA-----------------DAIEEGDGKAViDPDL--CIGCGSCVQVCPVD 66
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
56-83 8.04e-03

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 37.88  E-value: 8.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 1726868578  56 CINCKRCEVACPSDVKIGDIIQRARAKY 83
Cdd:COG1453   333 CIECGACEERCPQGLDIPELLKEAHELL 360
 
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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