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Conserved domains on  [gi|1084824573|gb|OGQ58584|]
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hypothetical protein A3I75_07415 [Deltaproteobacteria bacterium RIFCSPLOWO2_02_FULL_50_16]

Protein Classification

4Fe-4S dicluster domain-containing protein( domain architecture ID 11586797)

4Fe-4S dicluster domain-containing protein such as Salmonella enterica thiosulfate reductase electron transfer subunit PhsB, a component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor

Gene Ontology:  GO:0016491|GO:0046872|GO:0051539
SCOP:  3000020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 14-231 1.73e-90

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


:

Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 264.01  E-value: 1.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNVAlptavsaskaRSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVP----------PGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGAT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPKWPkemvpslnPDVSCRTKGVVEKCTFCHHRLQKAReqakmen 173
Cdd:cd10551    71 YKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEF--------GEVPVRPKGVVEKCTFCYHRLDEGL------- 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084824573 174 relkpgeyLPACVEACPGQAMYFGDLEDETSEVTKLSREPRAFKLLEDLGTEPKVIYL 231
Cdd:cd10551   136 --------LPACVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 14-231 1.73e-90

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 264.01  E-value: 1.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNVAlptavsaskaRSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVP----------PGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGAT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPKWPkemvpslnPDVSCRTKGVVEKCTFCHHRLQKAReqakmen 173
Cdd:cd10551    71 YKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEF--------GEVPVRPKGVVEKCTFCYHRLDEGL------- 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084824573 174 relkpgeyLPACVEACPGQAMYFGDLEDETSEVTKLSREPRAFKLLEDLGTEPKVIYL 231
Cdd:cd10551   136 --------LPACVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 8-231 9.10e-75

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 224.44  E-value: 9.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573   8 NMPKWGMVIDLDKCSACQACVTACHLENNVAlptavsaskaRSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKV 87
Cdd:COG0437     2 SMKRYGMVIDLTKCIGCRACVVACKEENNLP----------VGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  88 CPVKATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNwsepkwpkemvpslnpdvscRTKGVVEKCTFCHHRLQKARE 167
Cdd:COG0437    72 CPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFN--------------------PETGVVEKCTFCADRLDEGLL 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084824573 168 qakmenrelkpgeylPACVEACPGQAMYFGDLEDETSEVTKLSREPRAFKLLEDLGTEPKVIYL 231
Cdd:COG0437   132 ---------------PACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYL 180
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
11-232 1.98e-40

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 138.85  E-value: 1.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  11 KWGMVIDLDKCSACQACVTACHLENnvALPTAVSASKARSiYWIQMLPMKEgryphFKMKMIPVLCFHCEHPPCTKVCPV 90
Cdd:PRK14993   43 RYAMLIDLRRCIGCQSCTVSCTIEN--QTPQGAFRTTVNQ-YQVQREGSQE-----VTNVLLPRLCNHCDNPPCVPVCPV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  91 KATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSepkwpkemvpslnpdvscrTKgVVEKCTFCHHRLQKAreqak 170
Cdd:PRK14993  115 QATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHE-------------------TQ-TADKCTFCVHRLEAG----- 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084824573 171 menrelkpgeYLPACVEACPGQAMYFGDLEDETSEVTKLSREPRA-FKLLE-DLGTEPKVIYLG 232
Cdd:PRK14993  170 ----------LLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDaIKVLKpENGTSPHVFYLG 223
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 68-199 2.29e-18

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 76.90  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  68 KMKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvsc 146
Cdd:pfam13247   2 DWLFFPEQCRHCLNPPCKASCPVGAIYKDEEtGAVLLDEKTCRGWRECVSACPYNIPRYND------------------- 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084824573 147 rTKGVVEKCTFCHHRLQKAReqakmenrelkpgeyLPACVEACPGQAMYFGDL 199
Cdd:pfam13247  63 -ETGKAEKCDMCYDRVEAGL---------------LPACVQTCPTGAMNFGDR 99
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 62-212 6.17e-14

nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain. [Energy metabolism, Anaerobic]


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 70.28  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  62 GRYPHFKMKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPKwpkemvpsl 140
Cdd:TIGR01660 169 GEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEdGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGK--------- 239

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084824573 141 npdvscrtkgvVEKCTFCHHRLQKAreqakmenrelkpgeyLPA-CVEACPGQAMYFGDL---EDETSEVTKLSRE 212
Cdd:TIGR01660 240 -----------SEKCIFCYPRIEAG----------------QPTvCSETCVGRIRYLGVLlydADKIEEAASTENE 288
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 14-231 1.73e-90

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 264.01  E-value: 1.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNVAlptavsaskaRSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVP----------PGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGAT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPKWPkemvpslnPDVSCRTKGVVEKCTFCHHRLQKAReqakmen 173
Cdd:cd10551    71 YKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEF--------GEVPVRPKGVVEKCTFCYHRLDEGL------- 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084824573 174 relkpgeyLPACVEACPGQAMYFGDLEDETSEVTKLSREPRAFKLLEDLGTEPKVIYL 231
Cdd:cd10551   136 --------LPACVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 8-231 9.10e-75

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 224.44  E-value: 9.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573   8 NMPKWGMVIDLDKCSACQACVTACHLENNVAlptavsaskaRSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKV 87
Cdd:COG0437     2 SMKRYGMVIDLTKCIGCRACVVACKEENNLP----------VGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  88 CPVKATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNwsepkwpkemvpslnpdvscRTKGVVEKCTFCHHRLQKARE 167
Cdd:COG0437    72 CPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFN--------------------PETGVVEKCTFCADRLDEGLL 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084824573 168 qakmenrelkpgeylPACVEACPGQAMYFGDLEDETSEVTKLSREPRAFKLLEDLGTEPKVIYL 231
Cdd:COG0437   132 ---------------PACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYL 180
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
11-232 1.98e-40

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 138.85  E-value: 1.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  11 KWGMVIDLDKCSACQACVTACHLENnvALPTAVSASKARSiYWIQMLPMKEgryphFKMKMIPVLCFHCEHPPCTKVCPV 90
Cdd:PRK14993   43 RYAMLIDLRRCIGCQSCTVSCTIEN--QTPQGAFRTTVNQ-YQVQREGSQE-----VTNVLLPRLCNHCDNPPCVPVCPV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  91 KATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSepkwpkemvpslnpdvscrTKgVVEKCTFCHHRLQKAreqak 170
Cdd:PRK14993  115 QATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHE-------------------TQ-TADKCTFCVHRLEAG----- 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084824573 171 menrelkpgeYLPACVEACPGQAMYFGDLEDETSEVTKLSREPRA-FKLLE-DLGTEPKVIYLG 232
Cdd:PRK14993  170 ----------LLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDaIKVLKpENGTSPHVFYLG 223
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 13-197 1.15e-37

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 128.45  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTACHLENNVAlptavsaskaRSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKVCPVKA 92
Cdd:cd16371     1 GFYFDQERCIGCKACEIACKDKNDLP----------PGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  93 TYQNPEGIVGQIYKRCIGCRYCTTACPYTvrhfnwsepkwpkemVPSLNPDvscrtKGVVEKCTFCHHRLQKareqakme 172
Cdd:cd16371    71 ITKREDGIVVVDQDKCIGCGYCVWACPYG---------------APQYNPE-----TGKMDKCDMCVDRLDE-------- 122

                         170       180
                  ....*....|....*....|....*
gi 1084824573 173 nrelkpGEyLPACVEACPGQAMYFG 197
Cdd:cd16371   123 ------GE-KPACVAACPTRALDFG 140
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 14-232 1.86e-36

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 126.67  E-value: 1.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNVALPTAVSASKARS-IYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKVCPVKA 92
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKDEHVGNDWPGYAAPQPRHgHFWMRILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  93 TYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNwsepkwpkemvpslnpdvscRTKGVVEKCTFCHHRLQKareqakme 172
Cdd:cd10552    81 VYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWN--------------------EELQVPQKCTFCAHLLDD-------- 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573 173 nrelkpGEYLPACVEACPGQAMYFGDLEDEtsEVTKLSREPRAFKLLEDLGTEPKVIYLG 232
Cdd:cd10552   133 ------GWKEPRCVQACPTGALRFGKLEDE--EMAAKAAEEGLEVLHPELGTKPRVYYKN 184
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 13-201 5.71e-36

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 125.79  E-value: 5.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTACHLENNVALP----------TAVSASKARSIywIQMLPMKEGRY-PHFKMKMipvlCFHCEH 81
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAEdtafgpgwdnPRDLSAKTYTV--IKRYEVETGGKgFVFVKRQ----CMHCLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  82 PPCTKVCPVKATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPkWPKemvpslnpdvscrtkgvVEKCTFCHHR 161
Cdd:cd10561    75 PACVSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYEWDSA-NPK-----------------IRKCTMCYDR 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1084824573 162 LQKAREqakmenrelkpgeylPACVEACPGQAMYFGDLED 201
Cdd:cd10561   137 LKEGKQ---------------PACVEACPTGALLFGKREE 161
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 14-197 1.05e-35

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 123.27  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNvaLPTAVSASKARSIywiqmlpmkegRYPHFKMKMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHG--LRPGPDWSRIKVI-----------EGGGLERAFLPVSCMHCEDPPCVKACPTGAI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPEGIVgQIYK-RCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvscrTKGVVEKCTFCHHRLQKAREqakme 172
Cdd:cd04410    68 YKDEDGIV-LIDEdKCIGCGSCVEACPYGAIVFDP--------------------EPGKAVKCDLCGDRLDEGLE----- 121

                         170       180
                  ....*....|....*....|....*
gi 1084824573 173 nrelkpgeylPACVEACPGQAMYFG 197
Cdd:cd04410   122 ----------PACVKACPTGALTFG 136
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 14-197 3.36e-27

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 101.71  E-value: 3.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNV-ALPTAVSASKAR----SIYWIQMLPMKEGRYP--HFKMKMIPVLCFHCEHPPCTK 86
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNGLpAEKTEFTGSYQNppdlTAHTWTLVRFYEVEKPggDLSWLFRKDQCMHCTDAGCLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  87 VCPVKATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEpkwpkemvpslnpdvscrtkGVVEKCTFCHHRLQKAR 166
Cdd:cd16366    81 ACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEET--------------------GRVAKCTLCYDRISNGL 140

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1084824573 167 EqakmenrelkpgeylPACVEACPGQAMYFG 197
Cdd:cd16366   141 Q---------------PACVKTCPTGALTFG 156
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
13-205 6.76e-27

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 105.14  E-value: 6.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTACHLENNVALPTAVSA---------SKARSIywIQMLP--------MKEGRYPHFKMKmipvl 75
Cdd:PRK10882   39 GMLYDSTLCVGCQACVTKCQEINFPERNPQGEQtwdnpdklsPYTNNI--IKVWKsgtgvnkdQEENGYAYIKKQ----- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  76 CFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPkwpkemvpslnpdvscrtKGVVEK 154
Cdd:PRK10882  112 CMHCVDPNCVSVCPVSALTKDPKtGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNP------------------FGAIHK 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084824573 155 CTFCHHRLQKAREQAKMenrelkpgeylPACVEACPGQAMYFGDLEDETSE 205
Cdd:PRK10882  174 CELCNQKGVERLDKGGL-----------PGCVEVCPTGAVIFGTREELLAE 213
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 62-230 2.36e-25

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 100.84  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  62 GRYPHFKMKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNwsepkwpkemvpsl 140
Cdd:cd10555   119 GEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEdGIVLVDQDRCRGYRYCVEACPYKKIYFN-------------- 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573 141 npdvscRTKGVVEKCTFCHHRLQKAREqakmenrelkpgeylPACVEACPGQAMYFGDLEDETSEVTKLSREPR-AFKLL 219
Cdd:cd10555   185 ------PVEQKSEKCIFCYPRIEKGVA---------------PACARQCVGRIRFVGYLDDEESPVYKLVKKWKvALPLH 243

                         170
                  ....*....|.
gi 1084824573 220 EDLGTEPKVIY 230
Cdd:cd10555   244 PEYGTEPNVFY 254
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 16-201 2.43e-23

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 91.18  E-value: 2.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  16 IDLDKCSACQACVTACHLENNvalptavsaSKARsiywIQMLPMKEGryphfkmKMIPVLCFHCEHPPCTKVCPVKATYQ 95
Cdd:cd16374     3 VDPERCIGCRACEIACAREHS---------GKPR----ISVEVVEDL-------ASVPVRCRHCEDAPCMEVCPTGAIYR 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  96 NPEGIVGQIYKRCIGCRYCTTACPYTvrhfnwsepkwpkemVPSLNPDvscrtKGVVEKCTFCHHRLQKAREqakmenre 175
Cdd:cd16374    63 DEDGAVLVDPDKCIGCGMCAMACPFG---------------VPRFDPS-----LKVAVKCDLCIDRRREGKL-------- 114

                         170       180
                  ....*....|....*....|....*.
gi 1084824573 176 lkpgeylPACVEACPGQAMYFGDLED 201
Cdd:cd16374   115 -------PACVEACPTGALKFGDIEE 133
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 13-231 4.23e-23

beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 92.65  E-value: 4.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTACHlennvalpTAVSASKARSIYWIQMLPMKEGR-YPH-------------FKMKMIPVLCFH 78
Cdd:cd16365     4 AAVFNLNKCIGCQTCTVACK--------NAWTYRKGQEYMWWNNVETKPGGgYPQdwevktidnggntRFFFYLQRLCNH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  79 CEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvscrTKGVVEKCTF 157
Cdd:cd16365    76 CTNPACLAACPRGAIYKREEdGIVLIDQKRCRGYRKCVEQCPYKKIYFNG--------------------LSRVSEKCIA 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084824573 158 CHHRLQKAREQakmenrelkpgeylpACVEACPGQAMYFGDLEDE-TSEVTKLSREPR-AFKLLEDLGTEPKVIYL 231
Cdd:cd16365   136 CYPRIEGGDPT---------------RCMSACVGRIRLQGFLDDNpKSPVTKLIRHWKvALPLHPEYGTEPNIYYV 196
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 13-201 8.32e-23

beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 92.06  E-value: 8.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTACHLENnvALPT--------------AVSASKARSIYWIQMLPMKEGRYPHFKMK--MIPVLC 76
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWN--QLPAdgydfsgmsydntgDLSASTWRHVKFIERPTEDGPANEGGDLQwlFMSDVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  77 FHCEHPPCTKVCPVKATYQNPEGIVGQIYKRCIGCRYCTTACPYTVrhfnwsepkwpkemvpslnPDVSCRTkGVVEKCT 156
Cdd:cd10560    79 KHCTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGV-------------------IDRNEET-GRAHKCT 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1084824573 157 FCHHRLQKAREqakmenrelkpgeylPACVEACPGQAMYFGDLED 201
Cdd:cd10560   139 LCYDRLKDGLE---------------PACAKACPTGSIQFGPLEE 168
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 14-201 1.07e-22

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 90.44  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNV-ALPTAVSAS---------KARSIywIQMLPMKEGRYPhFKMKMIPVLCFHCEHPP 83
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNQLpAEKTPFTGSyqnppdltpNTWTL--IRFYEHEEDNGG-IRWLFRKRQCMHCTDAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  84 CTKVCPVKATYQNPEGIVGQIYKRCIGCRYCTTACPYTVRHFNwsepkwpkemvpslnpdvscRTKGVVEKCTFCHHRLQ 163
Cdd:cd10562    78 CVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYD--------------------ETTNKITKCTLCFDRIE 137

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1084824573 164 KAreqakmenrelkpgeYLPACVEACPGQAMYFGDLED 201
Cdd:cd10562   138 NG---------------MQPACVKTCPTGALTFGDRDE 160
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 14-196 1.70e-21

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 86.09  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNvalpTAVSASKARsiywIQMLPMKEGRYphfkmkMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd10550     1 LVVDPEKCTGCRTCELACSLKHE----GVFNPSLSR----IRVVRFEPEGL------DVPVVCRQCEDAPCVEACPVGAI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvscrTKGVVEKCTFCHhrlqkareqakme 172
Cdd:cd10550    67 SRDEEtGAVVVDEDKCIGCGMCVEACPFGAIRVDP--------------------ETGKAIKCDLCG------------- 113

                         170       180
                  ....*....|....*....|....
gi 1084824573 173 nrelkpGEylPACVEACPGQAMYF 196
Cdd:cd10550   114 ------GD--PACVKVCPTGALEF 129
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
15-198 6.34e-21

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 85.09  E-value: 6.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  15 VIDLDKCSACQACVTACHLENNvalptavSASKARSIYWIQMLPMKEGRyphfkmkmIPVLCFHCEHPPCTKVCPVKATY 94
Cdd:COG1142     6 IADPEKCIGCRTCEAACAVAHE-------GEEGEPFLPRIRVVRKAGVS--------APVQCRHCEDAPCAEVCPVGAIT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  95 QNpEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPkwpkemvpslnpdvscrtKGVVEKCTFCHHRlqkareqakmenr 174
Cdd:COG1142    71 RD-DGAVVVDEEKCIGCGLCVLACPFGAITMVGEKS------------------RAVAVKCDLCGGR------------- 118

                         170       180
                  ....*....|....*....|....
gi 1084824573 175 elkpgEYLPACVEACPGQAMYFGD 198
Cdd:COG1142   119 -----EGGPACVEACPTGALRLVD 137
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 16-205 1.44e-20

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 85.90  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  16 IDLDKCSACQACVTACHLENNvaLPTAVSASKA-----RSIYWIQMLPMKEGRYPH---FKMKMIPVLCFHCEHPPCTKV 87
Cdd:cd10558     4 IDVSKCIGCKACQVACKEWND--LRAEVGHNVGtyqnpADLSPETWTLMKFREVEDngkLEWLIRKDGCMHCADPGCLKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  88 CP-VKATYQNPEGIVGQIYKRCIGCRYCTTACPytvrhFNwsepkwpkemVPSLNPDvscrtKGVVEKCTFCHHRLQKAR 166
Cdd:cd10558    82 CPsPGAIVQYANGIVDFQSDKCIGCGYCIKGCP-----FD----------IPRISKD-----DNKMYKCTLCSDRVSVGL 141

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1084824573 167 EqakmenrelkpgeylPACVEACPGQAMYFGDLEDETSE 205
Cdd:cd10558   142 E---------------PACVKTCPTGALHFGTKEDMLAL 165
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 13-211 3.35e-20

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 84.78  E-value: 3.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQ-----ACVTACHLENNVALPTAVSA--------------SKARSIY-------WI--QMLPMKEGRy 64
Cdd:cd16368     2 ATLIDLTKCDGCPgesipACVRACREKNQARFPEPVSKpiqpywprkriedwSDKRDVTdrltpynWLyvQKLTVDTAG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  65 pHFKMKMIPVLCFHCEHPPCTKVCPVKATYQNPEGIVGQIYKRCIGCRYCTTACPytvrhfnWSEPKWPKEMVPSLNPDV 144
Cdd:cd16368    81 -GEKEVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCP-------WHIPQRQAGVGIYLHLAP 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084824573 145 SCRTKGVVEKCTFCHHRLQKAREqakmenrelkpgeylPACVEACPGQAMYFGdledETSEVTKLSR 211
Cdd:cd16368   153 EYAGGGVMYKCDLCKDLLAQGKP---------------PACIEACPKGAQYFG----PRKEMVALAR 200
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 14-200 1.67e-19

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 82.05  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTAChlennvalpTAVSASKARSIYWIQMLPmkegryPHFKMKMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd16369     4 FFIDPSRCIGCRACVAAC---------RECGTHRGKSMIHVDYID------RGESTQTAPTVCMHCEDPTCAEVCPADAI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPEGIVGQIYK-RCIGCRYCTTACPYTVrhfnwsePKWPKEMvpslnpdvscrtkGVVEKCTFCHHRLQKAREqakme 172
Cdd:cd16369    69 KVTEDGVVQSALKpRCIGCSNCVNACPFGV-------PKYDEER-------------NLMMKCDMCYDRTSVGKA----- 123

                         170       180
                  ....*....|....*....|....*...
gi 1084824573 173 nrelkpgeylPACVEACPGQAMYFGDLE 200
Cdd:cd16369   124 ----------PMCASVCPSGALFYGTRE 141
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 15-193 3.89e-19

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 80.38  E-value: 3.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  15 VIDLDKCSACQACVTAC---HLENNVALPTAVSASKARSIYWIQMLPMKegryphfkmkmIPVLCFHCEHPPCTKVCPVK 91
Cdd:cd10554     3 IADPDKCIGCRTCEVACaaaHSGKGIFEAGTDGLPFLPRLRVVKTGEVT-----------APVQCRQCEDAPCANVCPVG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  92 ATYQNpEGIVgQIY-KRCIGCRYCTTACPY-TVrhfnwsepkwpkEMVPSLNPDVSCR--TKGVVEKCTFCHHRLQKare 167
Cdd:cd10554    72 AISQE-DGVV-QVDeERCIGCKLCVLACPFgAI------------EMAPTTVPGVDWErgPRAVAVKCDLCAGREGG--- 134

                         170       180
                  ....*....|....*....|....*.
gi 1084824573 168 qakmenrelkpgeylPACVEACPGQA 193
Cdd:cd10554   135 ---------------PACVEACPTKA 145
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 17-197 1.46e-18

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 78.94  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  17 DLDKCSACQACVTACHLENNvaLPTAVSASKArsiywIQMLPMKEGRYPHFKMKMIPvlCFHCEHPPCTKVCPVKATYQ- 95
Cdd:cd10553     8 DSKRCIGCLACEVHCKVKNN--LPVGPRLCRI-----FAVGPKMVGGKPRLKFVYMS--CFHCENPWCVKACPTGAMQKr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  96 NPEGIVGQIYKRCIGCRYCTTACPytvrhfnWSEPKWPKEMvpslnpdvscrtkGVVEKCTFCHHRLQKAREqakmenre 175
Cdd:cd10553    79 EKDGIVYVDQELCIGCKACIEACP-------WGIPQWNPAT-------------GKVVKCDYCMDRIDQGLK-------- 130

                         170       180
                  ....*....|....*....|..
gi 1084824573 176 lkpgeylPACVEACPGQAMYFG 197
Cdd:cd10553   131 -------PACVTGCTTHALSFV 145
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 68-199 2.29e-18

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 76.90  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  68 KMKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvsc 146
Cdd:pfam13247   2 DWLFFPEQCRHCLNPPCKASCPVGAIYKDEEtGAVLLDEKTCRGWRECVSACPYNIPRYND------------------- 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084824573 147 rTKGVVEKCTFCHHRLQKAReqakmenrelkpgeyLPACVEACPGQAMYFGDL 199
Cdd:pfam13247  63 -ETGKAEKCDMCYDRVEAGL---------------LPACVQTCPTGAMNFGDR 99
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 16-197 1.69e-16

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 73.44  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  16 IDLDKCSACQACVTAChlennvalptAVSASKARSIYWI---QMLPMK----EGRYPHFkmkmIPVLCFHCEHPPCTKVC 88
Cdd:cd10563     4 IDEEKCLGCKLCEVAC----------AVAHSKSKDLIKAkleKERPRPrirvEESGGRS----FPLQCRHCDEPPCVKAC 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  89 PVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVrhfnwsepkwpkemvpsLNPDVscrTKGVVEKCTFCHHRLQkare 167
Cdd:cd10563    70 MSGAMHKDPEtGIVIHDEEKCVGCWMCVMVCPYGA-----------------IRPDK---ERKVALKCDLCPDRET---- 125

                         170       180       190
                  ....*....|....*....|....*....|
gi 1084824573 168 qakmenrelkpgeylPACVEACPGQAMYFG 197
Cdd:cd10563   126 ---------------PACVEACPTGALVLE 140
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 69-197 5.72e-16

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 75.86  E-value: 5.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  69 MKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvscR 147
Cdd:cd10557   172 MFYLPRICNHCLNPACVAACPSGAIYKREEdGIVLIDQDRCRGWRMCVSACPYKKVYYNW-------------------K 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1084824573 148 TkGVVEKCTFCHHRLQKAreQAkmenrelkpgeylPACVEACPGQAMYFG 197
Cdd:cd10557   233 T-GKSEKCIFCYPRLEAG--QP-------------TVCSETCVGRIRYLG 266
PRK09898 PRK09898
ferredoxin-like protein;
8-158 2.96e-15

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 71.79  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573   8 NMPKWGMVIDLDKCSACQACVTACHLENNVALPTAVSASKARSIYWIQMLPMKEGRYPHFKMKMIPVLCFHCEHPPCTKV 87
Cdd:PRK09898   55 NTPKGVLVTQRARCTGCHRCEISCTNFNDGSVGTFFSRIKIHRNYFFGDNGVGSGGGLYGDLNYTADTCRQCKEPQCMNV 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084824573  88 CPVKA-TYQNPEGIVGQIYKRCIGCRYCTTACPYtvrhfnwsepkwpkeMVPSLNPDVSCRTkgvveKCTFC 158
Cdd:PRK09898  135 CPIGAiTWQQKEGCITVDHKRCIGCSACTTACPW---------------MMATVNTESKKSS-----KCVLC 186
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 20-214 5.03e-15

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 73.63  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  20 KCSACQACVTACHLENNvalptavsaskarsiywiqmlpmkEGRYP----HF--KMKMI-------PVLCFHCEHPPCTK 86
Cdd:PRK12769   11 QCLGCHACEIACVMAHN------------------------DEQHVlsqhHFhpRITVIkhqqqrsAVTCHHCEDAPCAR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  87 VCPVKATYQNPEGI-VGQiyKRCIGCRYCTTACPYTVrhfnwsepkwpkeMVPSLNPDVSCRTKGVVEKCTFCHHRLQKa 165
Cdd:PRK12769   67 SCPNGAISHVDDSIqVNQ--QKCIGCKSCVVACPFGT-------------MQIVLTPVAAGKVKATAHKCDLCAGRENG- 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1084824573 166 reqakmenrelkpgeylPACVEACPGQAMyfgDLEDETSeVTKLSREPR 214
Cdd:PRK12769  131 -----------------PACVENCPADAL---QLVTEQA-LSGMAKSRR 158
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 62-212 6.17e-14

nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain. [Energy metabolism, Anaerobic]


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 70.28  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  62 GRYPHFKMKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPKwpkemvpsl 140
Cdd:TIGR01660 169 GEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEdGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGK--------- 239

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084824573 141 npdvscrtkgvVEKCTFCHHRLQKAreqakmenrelkpgeyLPA-CVEACPGQAMYFGDL---EDETSEVTKLSRE 212
Cdd:TIGR01660 240 -----------SEKCIFCYPRIEAG----------------QPTvCSETCVGRIRYLGVLlydADKIEEAASTENE 288
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 72-231 5.28e-13

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 66.71  E-value: 5.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  72 IPVLCFHCEHPPCTKVCPVKATYQNPE-GIVGQIYKRCIGCRYCTTACPYTVRHFNWsepkwpkemvpslnpdvscrTKG 150
Cdd:cd10556   137 LPRICNHCTYPACLAACPRKAIYKREEdGIVLIDQERCRGYRECVEACPYKKPMYNP--------------------TTR 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573 151 VVEKCTFCHHRLQKAREqakmenrelkpgeylPACVEACPGQAMYFGDL---------EDETSEVTKLSR-EPRAFKLLE 220
Cdd:cd10556   197 VSEKCIGCYPRIEEGDQ---------------TQCVSACIGKIRLQGFIntppdarwaDDRDNPIDFLVHiKKVALPLYP 261

                         170
                  ....*....|.
gi 1084824573 221 DLGTEPKVIYL 231
Cdd:cd10556   262 QFGTEPNVYYI 272
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 14-201 5.68e-13

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 63.87  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHlennvalptAVSASKARsiywiqmLPMKEGRYPHFkmkMIPVLCFHCEHPPCTKVCPVKAT 93
Cdd:cd16367    14 LVIDLDRCIRCDNCEKACA---------DTHDGHSR-------LDRNGLRFGNL---LVPTACRHCVDPVCMIGCPTGAI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  94 YQNPEGIVgQIYKRCIGCRYCTTACPYTVrhfnwsepkwpKEMVpslnpdvscrtkgVVEKCTFCHhrlqkareqakmen 173
Cdd:cd16367    75 HRDDGGEV-VISDACCGCGNCASACPYGA-----------IQMV-------------RAVKCDLCA-------------- 115

                         170       180
                  ....*....|....*....|....*...
gi 1084824573 174 relkpGEYLPACVEACPGQAMYFGDLED 201
Cdd:cd16367   116 -----GYAGPACVSACPTGAAIRVNPEE 138
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 69-197 2.67e-11

Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 62.52  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  69 MKMIPVLCFHCEHPPCTKVCPVKATYQNPE-GIV--GQiyKRCIGCRYCTTACPYTVRHFNWSEPKwpkemvpslnpdvs 145
Cdd:COG1140   175 MFYLPRICEHCLNPACVASCPSGAIYKREEdGIVlvDQ--DKCRGWRMCVSGCPYKKVYFNWKTGK-------------- 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1084824573 146 crtkgvVEKCTFCHHRLqkareqakmENRElkPgeylPACVEACPGQAMYFG 197
Cdd:COG1140   239 ------AEKCIFCYPRI---------EAGQ--P----TVCSETCVGRIRYLG 269
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 14-198 5.15e-11

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 61.58  E-value: 5.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTACHLENNVAlptavSASKARSIYWIQMLPMKEGRYPHfkmkmiPVLCFHCEHPPCTKVCPVKA- 92
Cdd:PRK12809    5 IAAEAAECIGCHACEIACAVAHNQE-----NWPLSHSDFRPRIHVVGKGQAAN------PVACHHCNNAPCVTACPVNAl 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  93 TYQNPEgiVGQIYKRCIGCRYCTTACPYTVrhfnwsepkwpKEMVPSLnpdvscrtkgvVEKCTFCHHRLQKAReqakme 172
Cdd:PRK12809   74 TFQSDS--VQLDEQKCIGCKRCAIACPFGV-----------VEMVDTI-----------AQKCDLCNQRSSGTQ------ 123

                         170       180
                  ....*....|....*....|....*.
gi 1084824573 173 nrelkpgeylpACVEACPGQAMYFGD 198
Cdd:PRK12809  124 -----------ACIEVCPTQALRLMD 138
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 15-126 6.04e-10

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 55.36  E-value: 6.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  15 VIDLDKCSACQACVTACHLENNVALPTAVSASKARSiywiqmlpmkegrYPHFKMKMIPVLCFHCEHPPCTKVCPVKATY 94
Cdd:cd16370     5 VKDMERCIGCYSCMLACSRRVHKSASLSKSAIRVRT-------------RGGLEGGFTVVVCRACEDPPCAEACPTGALE 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1084824573  95 QNPEGIVGQIYKRCIGCRYCTTACPYTVRHFN 126
Cdd:cd16370    72 PRKGGGVVLDKEKCIGCGNCVKACIVGAIFWD 103
PRK10330 PRK10330
electron transport protein HydN;
14-194 8.57e-10

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 56.05  E-value: 8.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  14 MVIDLDKCSACQACVTAC---HLENNvALPTAVSASKARSIYWIQMLPMKEGryphfkmkmipVLCFHCEHPPCTKVCPV 90
Cdd:PRK10330    5 IIADASKCIGCRTCEVACvvsHQENQ-DCASLTPETFLPRIHVIKGVNVSTA-----------TVCRQCEDAPCANVCPN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  91 KATYQNpEGIVGQIYKRCIGCRYCTTACPY---------TVRHFNWSEPkwpkemvpslnpdvSCRTKGVVEKCTFCHHR 161
Cdd:PRK10330   73 GAISRD-KGFVHVMQERCIGCKTCVVACPYgamevvvrpVIRNSGAGLN--------------VRAEKAEANKCDLCNHR 137

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1084824573 162 lqkareqakmenrelkpgEYLPACVEACPGQAM 194
Cdd:PRK10330  138 ------------------EDGPACMAACPTHAL 152
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 13-201 2.32e-09

tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 55.13  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTACHLEN-NVALPTAVSASKAR----SIYWIQMLPMKEGRYPHFKMKM--IPVLCFHCEHPPCT 85
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWNqLPAEQTKNTGSHQNppdlSANTYKLVRFNEVRNENGKPDWlfFPDQCRHCVTPPCK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  86 KVCPVKA---TYQNPEGIVGQIYKRCIGCRYCTT-ACPYTVrhfnwsepkwpkemvPSLNPDvscrtKGVVEKCTFCHHR 161
Cdd:cd10559    81 DAADMVPgavIQDEATGAVVFTEKTAELDFDDVLsACPYNI---------------PRKNEA-----TGRIVKCDMCIDR 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1084824573 162 LqkareqakmenrelKPGeYLPACVEACPGQAMYFGDLED 201
Cdd:cd10559   141 V--------------SNG-LQPACVKACPTGAMNFGDRDE 165
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 13-119 5.63e-06

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: 44.31  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  13 GMVIDLDKCSACQACVTAChlennvalPTAVsaskarsiywIQMLPMKEGRYPHFKMKMI-PVLCFHCEHppCTKVCPVK 91
Cdd:cd10549    34 GPEIDEDKCVFCGACVEVC--------PTGA----------IELTPEGKEYVPKEKEAEIdEEKCIGCGL--CVKVCPVD 93

                          90       100
                  ....*....|....*....|....*....
gi 1084824573  92 A-TYQNPEGIVgQIYKRCIGCRYCTTACP 119
Cdd:cd10549    94 AiTLEDELEIV-IDKEKCIGCGICAEVCP 121
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
68-131 6.53e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.10  E-value: 6.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084824573  68 KMKMIPVLCFHCEHppCTKVCPVKATYQNpEGIVGQIYKRCIGCRYCTTACPYTVRHFNWSEPK 131
Cdd:COG2768     5 KPYVDEEKCIGCGA--CVKVCPVGAISIE-DGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDE 65
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 15-120 8.19e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.17  E-value: 8.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  15 VIDLDKCSACQACVTAChlennvalPTAVSASKARSIYWIQMLPMKEGryphfkmkMIPVLCFHCEHppCTKVCPVKATY 94
Cdd:cd16372     4 VTDPEKCIGCLQCEEAC--------SKTFFKEEDREKSCIRITETEGG--------YAINVCNQCGE--CIDVCPTGAIT 65

                          90       100
                  ....*....|....*....|....*.
gi 1084824573  95 QNPEGIVGQIYKRCIGCRYCTTACPY 120
Cdd:cd16372    66 RDANGVVMINKKLCVGCLMCVGFCPE 91
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
76-119 6.46e-04

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 40.39  E-value: 6.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1084824573  76 CFHCEhpPCTKVCPVKATYQNpEGIVGQIYKRCIGCRYCTTACP 119
Cdd:COG4624    93 CKNCY--PCVRACPVKAIKVD-DGKAEIDEEKCISCGQCVAVCP 133
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 68-119 1.03e-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: 36.46  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084824573  68 KMKMIPVLCFHCEhpPCTKVCP-----VKATYQNPEGIVGQI-YKRCIGCRYCTTACP 119
Cdd:pfam13237   1 KVVIDPDKCIGCG--RCTAACPagltrVGAIVERLEGEAVRIgVWKCIGCGACVEACP 56
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
98-202 1.04e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.84  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  98 EGIVGQI-YKRCIGCRYCTTACPYTVRHFNwsepkwpKEMVPSLNPdVSCRTKGvvekctfchhrlqkareqakmenrel 176
Cdd:COG1148   487 EPSVAEVdPEKCTGCGRCVEVCPYGAISID-------EKGVAEVNP-ALCKGCG-------------------------- 532

                          90       100
                  ....*....|....*....|....*.
gi 1084824573 177 kpgeylpACVEACPGQAMYFGDLEDE 202
Cdd:COG1148   533 -------TCAAACPSGAISLKGFTDD 551
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
15-119 1.09e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.15  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  15 VIDLDKCSACQACVTAChlennvalPTAV-SASKARSIYWIQMLPMKEGRyphFKMKMIPVLCFHCEHppCTKVCPVKA- 92
Cdd:PRK07118  164 VVDEDKCTGCGACVKAC--------PRNViELIPKSARVFVACNSKDKGK---AVKKVCEVGCIGCGK--CVKACPAGAi 230

                          90       100
                  ....*....|....*....|....*..
gi 1084824573  93 TYQNpeGIVGQIYKRCIGCRYCTTACP 119
Cdd:PRK07118  231 TMEN--NLAVIDQEKCTSCGKCVEKCP 255
PRK13795 PRK13795
hypothetical protein; Provisional
 84-119 1.22e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.59  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1084824573  84 CTKVCPVKA-TYQNPEGIVGQIYKRCIGCRYCTTACP 119
Cdd:PRK13795  589 CVGACPTGAiRIEEGKRKISVDEEKCIHCGKCTEVCP 625
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 15-119 1.49e-03

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 38.82  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084824573  15 VIDLDKCSACQACVTAChlennvalPTAVsaskarsiywIQMLPMKEGRYPHFKMKMIPVL-CFHCEHPPCTKVCPVKAT 93
Cdd:COG2878   163 TVDEDKCTGCGLCVEAC--------PVDC----------IEMVPVSPTVVVSSWDKGKAVRkVVGCIGLCCKKCCPAAAI 224

                          90       100
                  ....*....|....*....|....*.
gi 1084824573  94 YQNpEGIVGQIYKRCIGCRYCTTACP 119
Cdd:COG2878   225 TVN-NLAAIIDYKKCTCCGCCEKCCP 249
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
84-119 1.99e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 36.85  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1084824573  84 CTKVCPVKATYQNPEGIVGQIYKRCIGCRYCTTACP 119
Cdd:PRK09623   59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECP 94
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 84-119 2.87e-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: 35.11  E-value: 2.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1084824573  84 CTKVCPVKATYQNPEGIVGQI---YKRCIGCRYCTTACP 119
Cdd:COG1143    10 CVRVCPVDAITIEDGEPGKVYvidPDKCIGCGLCVEVCP 48
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 75-119 7.15e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 37.16  E-value: 7.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1084824573  75 LCFHCEHppCTKVCPVKATYQNPEGIVGQI-YKRCIGCRYCTTACP 119
Cdd:PRK12771  511 NCFECDN--CYGACPQDAIIKLGPGRRYHFdYDKCTGCHICADVCP 554
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 71-119 7.63e-03

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: 34.64  E-value: 7.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084824573  71 MIPVL----CFHCEhpPCTKVCPVKATYQNPEGIVGQIYKRCIGCRYCTTACP 119
Cdd:COG1144    23 ERPVVdedkCIGCG--LCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCP 73
 
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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