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Conserved domains on  [gi|1950807618|gb|QQG35121|]
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succinate dehydrogenase/fumarate reductase iron-sulfur subunit [Deltaproteobacteria bacterium]

Protein Classification

succinate dehydrogenase/fumarate reductase iron-sulfur subunit( domain architecture ID 11482816)

succinate dehydrogenase/fumarate reductase iron-sulfur subunit is a membrane-bound, FAD-containing enzyme that catalyzes the interconversion of fumarate and succinate; fumarate reductase is used in anaerobic growth while succinate dehydrogenase is used in aerobic growth

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 3-233 3.37e-157

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


:

Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 435.42  E-value: 3.37e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618   3 GAFVTENISGISPDMSFLEMLDILNDRILSRNDHPVCFESDCREGICGACSLVINGVAHGRQTGTTTCQLHMRSFKSGST 82
Cdd:PRK07570   17 GKFETYEVDDISPDMSFLEMLDVLNEQLIEKGEEPVAFDHDCREGICGMCGLVINGRPHGPDRGTTTCQLHMRSFKDGDT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  83 IVVEPFRARSFPVIRDLVVDRSALDRIMQAGGYISVNVGSAPDAHSILVDKKSADQAFEAAACIGCGACVAMCKNSSAML 162
Cdd:PRK07570   97 ITIEPWRAAAFPVIKDLVVDRSALDRIIQAGGYVSVNTGGAPDANAIPVPKEDADRAFDAAACIGCGACVAACPNGSAML 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807618 163 FVGAKISQLSKLPQGQPERYERVKRMVEQMQVEGFGGCSNTMACEAVCPKGITTKVISELNWEFLKMTLKS 233
Cdd:PRK07570  177 FTGAKVSHLALLPQGQPERARRVRAMVAQMDEEGFGNCTNTGECEAVCPKGISLENIARMNREYLRASFRG 247
 
Name Accession Description Interval E-value
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 3-233 3.37e-157

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 435.42  E-value: 3.37e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618   3 GAFVTENISGISPDMSFLEMLDILNDRILSRNDHPVCFESDCREGICGACSLVINGVAHGRQTGTTTCQLHMRSFKSGST 82
Cdd:PRK07570   17 GKFETYEVDDISPDMSFLEMLDVLNEQLIEKGEEPVAFDHDCREGICGMCGLVINGRPHGPDRGTTTCQLHMRSFKDGDT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  83 IVVEPFRARSFPVIRDLVVDRSALDRIMQAGGYISVNVGSAPDAHSILVDKKSADQAFEAAACIGCGACVAMCKNSSAML 162
Cdd:PRK07570   97 ITIEPWRAAAFPVIKDLVVDRSALDRIIQAGGYVSVNTGGAPDANAIPVPKEDADRAFDAAACIGCGACVAACPNGSAML 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807618 163 FVGAKISQLSKLPQGQPERYERVKRMVEQMQVEGFGGCSNTMACEAVCPKGITTKVISELNWEFLKMTLKS 233
Cdd:PRK07570  177 FTGAKVSHLALLPQGQPERARRVRAMVAQMDEEGFGNCTNTGECEAVCPKGISLENIARMNREYLRASFRG 247
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 13-228 2.48e-80

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: 240.03  E-value: 2.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  13 ISPDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKsgSTIVVEPFRArs 92
Cdd:COG0479    27 VSPGMTVLDALDYIKEEQ----DPTLAFRRSCREGICGSCAMVINGRP------RLACQTHVRDLK--DTITIEPLRN-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  93 FPVIRDLVVDRSAL-DRIMQAGGYISVNvGSAPDaHSILVDKKSADQAFEAAACIGCGACVAMCKNSSAML-FVGAKIS- 169
Cdd:COG0479    93 FPVIKDLVVDRSAFfDKLKKVKPYLSPD-GPAPD-NERLQSPEDREKADDLAECILCGACVAACPNVWANPdFLGPAALa 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950807618 170 ---QLSKLPQGQpERYERVKRMveqMQVEGFGGCSNTMACEAVCPKGI-TTKVISELNWEFLK 228
Cdd:COG0479   171 qayRFALDPRDE-ETEERLEAL---EDEEGVWRCTTCGNCTEVCPKGIpPTKAIAKLKREALK 229
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 13-108 6.32e-22

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 86.52  E-value: 6.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  13 ISPDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKsGSTIVVEPFRArs 92
Cdd:pfam13085  25 YEEGMTVLDALNKIKEEQ----DPTLAFRRSCREGICGSCAMNINGKP------RLACKTLIDDLL-GQDITLEPLPG-- 91

                          90
                  ....*....|....*.
gi 1950807618  93 FPVIRDLVVDRSALDR 108
Cdd:pfam13085  92 FPVIRDLVVDRSAFFE 107
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 15-214 3.15e-19

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: 82.48  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  15 PDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFkSGSTIVVEPFraRSFP 94
Cdd:TIGR00384  23 EGMTVLDALNYIKDEQ----DPSLAFRRSCRNGICGSCAMNVNGKP------VLACKTKVEDL-GQPVMKIEPL--PNLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  95 VIRDLVVDRS----ALDRIMQaggYISVNVGSAPDAHSILV--DKKSADQAFEaaaCIGCGACVAMC----KNSSamlFV 164
Cdd:TIGR00384  90 VIKDLVVDMGpfyaKLEAIKP---YLIRKSQPEPEGEFLQTpeQREKLDQLSG---CILCGCCYSSCpafwWNPE---FL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950807618 165 G-AKISQLSKL-----PQGQPERYErvkrmvEQMQVEGFGGCSNTMACEAVCPKGI 214
Cdd:TIGR00384 161 GpAALTAAYRFlidsrDHATKDRLE------GLNDKNGVWRCTTCMNCSEVCPKGV 210
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 137-228 3.94e-04

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: 41.24  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 137 DQAF--EAAACIGCGACVAMCKNS----SAMLFvgAKISQLSKLpqgqPERYERvkrmveqmqvegfggCSNTMACEAVC 210
Cdd:cd01916   357 DEEFqeLAAKCTDCGWCTRACPNSlrikEAMEA--AKEGDFSGL----ADLFDQ---------------CVGCGRCEQEC 415

                          90
                  ....*....|....*....
gi 1950807618 211 PKGI-TTKVISELNWEFLK 228
Cdd:cd01916   416 PKEIpIINMIEKAARERIK 434
 
Name Accession Description Interval E-value
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 3-233 3.37e-157

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 435.42  E-value: 3.37e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618   3 GAFVTENISGISPDMSFLEMLDILNDRILSRNDHPVCFESDCREGICGACSLVINGVAHGRQTGTTTCQLHMRSFKSGST 82
Cdd:PRK07570   17 GKFETYEVDDISPDMSFLEMLDVLNEQLIEKGEEPVAFDHDCREGICGMCGLVINGRPHGPDRGTTTCQLHMRSFKDGDT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  83 IVVEPFRARSFPVIRDLVVDRSALDRIMQAGGYISVNVGSAPDAHSILVDKKSADQAFEAAACIGCGACVAMCKNSSAML 162
Cdd:PRK07570   97 ITIEPWRAAAFPVIKDLVVDRSALDRIIQAGGYVSVNTGGAPDANAIPVPKEDADRAFDAAACIGCGACVAACPNGSAML 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807618 163 FVGAKISQLSKLPQGQPERYERVKRMVEQMQVEGFGGCSNTMACEAVCPKGITTKVISELNWEFLKMTLKS 233
Cdd:PRK07570  177 FTGAKVSHLALLPQGQPERARRVRAMVAQMDEEGFGNCTNTGECEAVCPKGISLENIARMNREYLRASFRG 247
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 13-228 2.48e-80

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: 240.03  E-value: 2.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  13 ISPDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKsgSTIVVEPFRArs 92
Cdd:COG0479    27 VSPGMTVLDALDYIKEEQ----DPTLAFRRSCREGICGSCAMVINGRP------RLACQTHVRDLK--DTITIEPLRN-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  93 FPVIRDLVVDRSAL-DRIMQAGGYISVNvGSAPDaHSILVDKKSADQAFEAAACIGCGACVAMCKNSSAML-FVGAKIS- 169
Cdd:COG0479    93 FPVIKDLVVDRSAFfDKLKKVKPYLSPD-GPAPD-NERLQSPEDREKADDLAECILCGACVAACPNVWANPdFLGPAALa 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950807618 170 ---QLSKLPQGQpERYERVKRMveqMQVEGFGGCSNTMACEAVCPKGI-TTKVISELNWEFLK 228
Cdd:COG0479   171 qayRFALDPRDE-ETEERLEAL---EDEEGVWRCTTCGNCTEVCPKGIpPTKAIAKLKREALK 229
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 37-233 3.00e-28

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 107.38  E-value: 3.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  37 PVCFESDCREGICGACSLVINGVAhgRQTGTTTCQLHMRSfksgstIVVEPFraRSFPVIRDLVVDRS----ALDRIMqa 112
Cdd:PRK08640   56 PVVWDMNCLEEVCGACSMVINGKP--RQACTALIDQLEQP------IRLEPM--STFPVVRDLQVDRSrmfdNLKRVK-- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 113 gGYISV----NVGSAPDahsilVDKKSADQAFEAAACIGCGACVAMCKN-SSAMLFVG-AKISQlSKL----PQGQPERY 182
Cdd:PRK08640  124 -AWIPIdgtyDLGPGPR-----MPEEKRQWAYELSKCMTCGCCLEACPNvNEKSDFIGpAAISQ-VRLfnahPTGEMHKE 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950807618 183 ERVKRMveqMQVEGFGGCSNTMACEAVCPKGIT-TKVISELNWEFLKMTLKS 233
Cdd:PRK08640  197 ERLRAL---MGDGGIADCGNAQNCVRVCPKGIPlTTSIAAMNRETTKQSFKS 245
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 13-108 6.32e-22

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 86.52  E-value: 6.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  13 ISPDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKsGSTIVVEPFRArs 92
Cdd:pfam13085  25 YEEGMTVLDALNKIKEEQ----DPTLAFRRSCREGICGSCAMNINGKP------RLACKTLIDDLL-GQDITLEPLPG-- 91

                          90
                  ....*....|....*.
gi 1950807618  93 FPVIRDLVVDRSALDR 108
Cdd:pfam13085  92 FPVIRDLVVDRSAFFE 107
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 15-214 3.15e-19

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: 82.48  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  15 PDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFkSGSTIVVEPFraRSFP 94
Cdd:TIGR00384  23 EGMTVLDALNYIKDEQ----DPSLAFRRSCRNGICGSCAMNVNGKP------VLACKTKVEDL-GQPVMKIEPL--PNLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  95 VIRDLVVDRS----ALDRIMQaggYISVNVGSAPDAHSILV--DKKSADQAFEaaaCIGCGACVAMC----KNSSamlFV 164
Cdd:TIGR00384  90 VIKDLVVDMGpfyaKLEAIKP---YLIRKSQPEPEGEFLQTpeQREKLDQLSG---CILCGCCYSSCpafwWNPE---FL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950807618 165 G-AKISQLSKL-----PQGQPERYErvkrmvEQMQVEGFGGCSNTMACEAVCPKGI 214
Cdd:TIGR00384 161 GpAALTAAYRFlidsrDHATKDRLE------GLNDKNGVWRCTTCMNCSEVCPKGV 210
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 44-228 1.83e-18

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 80.61  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  44 CREGICGACSLVINGvahgrqTGTTTCQLHMRSFKSGsTIVVEPFraRSFPVIRDLVVDRS----ALDRIMQaggYIsVN 119
Cdd:PRK05950   52 CREGVCGSDAMNING------KNGLACITPISDLKKG-KIVIRPL--PGLPVIKDLVVDMTqfyaQYRSIKP---YL-IN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 120 VGSAPDA---HSIlVDKKSADQAFEaaaCIGCGACVAMC----KNSSAmlFVG-AKISQLSKL-----PQGQPERYERVK 186
Cdd:PRK05950  119 DTPPPARerlQSP-EDREKLDGLYE---CILCACCSTSCpsfwWNPDK--FLGpAALLQAYRFiadsrDEATGERLDILD 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1950807618 187 rmveqmQVEGFGGCSNTMACEAVCPKGIT-TKVISELNWEFLK 228
Cdd:PRK05950  193 ------DPFGVFRCHTIMNCVEVCPKGLNpTKAIGEIKRMLLE 229
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 14-222 1.55e-15

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 75.04  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  14 SPDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGvahgrqTGTTTCqlhMRSFKSGSTIvvEPFRarsF 93
Cdd:PRK06259   28 KEGMTVLDALEYINKTY----DANIAFRSSCRAGQCGSCAVTING------EPVLAC---KTEVEDGMII--EPLD---F 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  94 PVIRDLVVDRSALDRIMQaggyiSVNVGSAPDAHSILVdKKSADQAFEAAACIGCGACVAMCKNSSAMLFVGAKI-SQLS 172
Cdd:PRK06259   90 PVIKDLIVDREPYYKKLK-----SLRNYLQRKNEKITY-PEDIEDIKKLRGCIECLSCVSTCPARKVSDYPGPTFmRQLA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950807618 173 KLPQGQPERYERVKRMVEqmqvEGFGGCSNTMACEAVCPKGITT--KVISEL 222
Cdd:PRK06259  164 RFAFDPRDEGDREKEAFD----EGLYNCTTCGKCVEVCPKEIDIpgKAIEKL 211
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 26-214 8.95e-15

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 70.75  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  26 LNdRILSRNDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKSGsTIVVEPFRArsFPVIRDLVVDRSA 105
Cdd:PRK13552   40 LN-RIREEQDPSLQFDFVCRAGICGSCAMVINGRP------TLACRTLTSDYPDG-VITLMPLPV--FKLIGDLSVNTGK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 106 LDRIMqaggyiSVNVGS------APDAHSI--LVDKKSADQAFEAAACIGCGACVAMCknSSAML---FVGAkiSQLSKL 174
Cdd:PRK13552  110 WFREM------SERVESwihtdkEFDIHRLeeRMEPEEADEIYELDRCIECGCCVAAC--GTKQMredFVGA--VGLNRI 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1950807618 175 PqgqpeRYE---RVKRMVEQM-----QVEGFGGCSNTMACEAVCPKGI 214
Cdd:PRK13552  180 A-----RFEldpRDERTDEDFyeligNDDGVFGCMSLLGCEDNCPKDL 222
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
19-214 1.37e-14

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 70.93  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  19 FLEMLDILNdRILSRNDHPVCFESDCREGICGACSLVINGvahgrqTGTTTCQ---LHMRSfKSGSTIVVEPFraRSFPV 95
Cdd:PRK12576   34 FTQVTEALR-RIKEEQDPTLSYRASCHMAVCGSCGMKING------EPRLACKtlvLDVAK-KYNSVITIEPM--DYFKV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  96 IRDLVVDRSALDRIMQAGG---YISVNVGSAPDAHSILVDKKSadQAFEAAACIGCGACVAMCKnssamlfvGAKISQLS 172
Cdd:PRK12576  104 VKDLIVDFDEFYERMFKVKprlYRAKEVLEGKAEHRLKPEDQK--ELWKFAQCIWCGLCVSACP--------VVAIDPEF 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1950807618 173 KLPQGQPERYE-----RVKRMVEQMQV--EGFGGCSNTMACEAVCPKGI 214
Cdd:PRK12576  174 LGPAAHAKGYRfladpRDTITEERMKIliDSSWRCTYCYSCSNVCPRDI 222
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
14-214 2.15e-12

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 64.34  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  14 SPDMSFLEMLDILNDRIlsrnDHPVCFESDCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKSGSTIvvEPFraRSF 93
Cdd:PRK12385   32 DETTSLLDALGYIKDNL----APDLSYRWSCRMAICGSCGMMVNNVP------KLACKTFLRDYTGGMKV--EAL--ANF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  94 PVIRDLVVDRSA-LDRIMQAGGYISVNVGSAPDAHSILVDKKSAdQAFEAAACIGCGACVAMCK----NSSamlFVG-AK 167
Cdd:PRK12385   98 PIERDLVVDMTHfIESLEAIKPYIIGNDRTPDDGPNKQTPAQMA-KYHQFSGCINCGLCYAACPqfglNPE---FIGpAA 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950807618 168 ISQLsklpqgqpERYE-------RVKRMVEQMQVEGFGGCSNTMACEAVCPKGI 214
Cdd:PRK12385  174 ITLA--------HRYNldsrdhgKKERMKQLNGQNGVWSCTFVGYCSEVCPKHV 219
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
23-214 1.03e-11

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 63.18  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  23 LDILNdRILSRNDHPVCFESDCREGICGACSLVING---VAHGRQTGTTTCQLHMRSFKSGSTIVVEPFraRSFPVIRDL 99
Cdd:PRK12577   32 LDCLN-RIKWEQDGSLAFRKNCRNTICGSCAMRINGrsaLACKENVGSELARLSDSNSGAIPEITIAPL--GNMPVIKDL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 100 VVDRSAL-DRIMQAGGYISVNVGSAPDAHSILV--DKKSADQafeAAACIGCGACVAMCK----NSSamlFVG----AKI 168
Cdd:PRK12577  109 VVDMSSFwQNLEAVDPYVSTAARQVPEREFLQTpeERSKLDQ---TGNCILCGACYSECNarevNPE---FVGphalAKA 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1950807618 169 SQLSklpqgQPERYERVKRMVEQMQVEGFG--GCSNTMACEAVCPKGI 214
Cdd:PRK12577  183 QRMV-----ADSRDTATEQRLELYNQGTAGvwGCTRCYYCNSVCPMEV 225
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
22-222 5.68e-11

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 60.36  E-value: 5.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  22 MLDILNDriLSRNDHPVCFESDCREGICGACSLVINGvahgrqTGTTTCQLHMRSFKsgSTIVVEPFRArsFPVIRDLVV 101
Cdd:PRK12575   36 LLDVLGR--VKAQDETLSYRRSCREGICGSDAMNING------RNGLACLTNMQALP--REIVLRPLPG--LPVVRDLIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 102 DRSALDRIMQAGGYISVNVGSAPDAHSILV--DKKSADQAFEaaaCIGCGACVAMCKNS--SAMLFVGakisqlsklPQG 177
Cdd:PRK12575  104 DMTDFFNQYHSIRPYLINDTVPPERERLQTpqEREQLDGLYE---CILCACCSTACPSYwwNPDKFVG---------PAG 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1950807618 178 QPERYERVKRMVEQMQVEGFGG---------CSNTMACEAVCPKGIT-TKVISEL 222
Cdd:PRK12575  172 LLQAYRFIADSRDDATAARLDDledpyrlfrCRTIMNCVDVCPKGLNpARAIGQI 226
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 22-214 1.91e-10

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 59.42  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  22 MLDILNdRILSRNDHPVCFESDCREGICGACSLVINGvahgrqTGTTTCQLHMRSFKSGSTIVVepfrarSFP---VIRD 98
Cdd:PLN00129   75 VLDVLI-KIKNEQDPSLTFRRSCREGICGSCAMNIDG------KNTLACLTKIDRDESGPTTIT------PLPhmfVIKD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  99 LVVDrsaLDRIMQAggYISV------NVGSAPDAHSIL---VDKKSADQAFEaaaCIGCGACVAMCK----NSSAmlFVG 165
Cdd:PLN00129  142 LVVD---MTNFYQQ--YKSIepwlktKKPPEDGQKEHLqskEDRAKLDGMYE---CILCACCSTSCPsywwNPEK--FLG 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950807618 166 -AKISQLSKLPQGQPERY--ERVKRMVEQMQVegfGGCSNTMACEAVCPKGI 214
Cdd:PLN00129  212 pAALLHAYRWISDSRDEYtkERLEALDDEFKL---YRCHTIRNCSNACPKGL 260
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 43-215 4.62e-10

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 57.79  E-value: 4.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618  43 DCREGICGACSLVINGVAhgrqtgTTTCQLHMRSFKSGSTIVVEPFRArsFPVIRDLVVDrsaldrimqaggyISVNVGS 122
Cdd:PRK12386   52 NCKAGKCGSCSAEINGRP------RLMCMTRMSTFDEDETVTVTPMRT--FPVIRDLVTD-------------VSFNYEK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 123 APDAHSILVDKKSA-----------DQAFEAAACIGCGACVAMC-------KNSSAmlFVGAK----ISQLSKLPQGQPE 180
Cdd:PRK12386  111 AREIPSFTPPKDLQpgeyrmqqvdvERSQEFRKCIECFLCQNVChvvrdheENKPA--FAGPRflmrIAELEMHPLDTAD 188

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1950807618 181 RYERVKrmveqmQVEGFGGCSNTMACEAVCPKGIT 215
Cdd:PRK12386  189 RRAEAQ------EEHGLGYCNITKCCTEVCPEHIK 217
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 144-214 6.52e-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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 39.99  E-value: 6.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807618 144 ACIGCGACVAMCknssamLFVGAKISQLSKLPQGQPERYERVKRMVEQmQVEGFGGCSNTMACEAVCPKGI 214
Cdd:pfam13183   1 RCIRCGACLAAC------PVYLVTGGRFPGDPRGGAAALLGRLEALEG-LAEGLWLCTLCGACTEVCPVGI 64
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
135-223 2.12e-04

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 41.78  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 135 SADQAFEAaaCIGCGACVAMCKNSSAM-LFVGAKisqlsklpQGQPErYERVKRMVEQMQVEGFGGCSNTMACEAVCPKG 213
Cdd:PRK11168    1 MSDTSFDS--CIKCTVCTTACPVARVNpLYPGPK--------QAGPD-GERLRLKDGALYDESLKYCSNCKRCEVACPSG 69

                          90
                  ....*....|
gi 1950807618 214 ITtkvISELN 223
Cdd:PRK11168   70 VK---IGDII 76
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 137-228 3.94e-04

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: 41.24  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 137 DQAF--EAAACIGCGACVAMCKNS----SAMLFvgAKISQLSKLpqgqPERYERvkrmveqmqvegfggCSNTMACEAVC 210
Cdd:cd01916   357 DEEFqeLAAKCTDCGWCTRACPNSlrikEAMEA--AKEGDFSGL----ADLFDQ---------------CVGCGRCEQEC 415

                          90
                  ....*....|....*....
gi 1950807618 211 PKGI-TTKVISELNWEFLK 228
Cdd:cd01916   416 PKEIpIINMIEKAARERIK 434
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 145-214 1.83e-03

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: 35.58  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807618 145 CIGCGACVAMCKNSSAMLfvgakisqlsklpqgqpeRYERVKRMVEQMQVEgFGGCSNTMACEAVCPKGI 214
Cdd:pfam12838   1 CIGCGACVAACPVGAITL------------------DEVGEKKGTKTVVID-PERCVGCGACVAVCPTGA 51
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 144-214 2.23e-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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 35.52  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807618 144 ACIGCGACVAMCknSSAMLFvgakisqlsKLPQGQPERYERVKRMVEQMQVEGFGGCSNTMACEAVCPKGI 214
Cdd:pfam13534   1 RCIQCGCCVDEC--PRYLLN---------GDEPKKLMRAAYLGDLEELQANKVANLCSECGLCEYACPMGL 60
 
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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