ID O29594_ARCFU Unreviewed; 404 AA.
AC O29594;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
GN OrderedLocusNames=AF_0663 {ECO:0000313|EMBL:AAB90578.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325 {ECO:0000313|EMBL:AAB90578.1, ECO:0000313|Proteomes:UP000002199};
RN [1] {ECO:0000313|EMBL:AAB90578.1, ECO:0000313|Proteomes:UP000002199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC {ECO:0000313|Proteomes:UP000002199};
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.P., Clayton R.A., Tomb J., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B., Peterson S.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L., Utterback T., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of
CC CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB
CC (coenzyme B). {ECO:0000256|RuleBase:RU366072}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU366072};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU366072};
CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC heterodisulfide: step 1/1. {ECO:0000256|RuleBase:RU366072}.
CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC of three subunits; HdrA, HdrB and HdrC.
CC {ECO:0000256|RuleBase:RU366072}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000256|ARBA:ARBA00006561,
CC ECO:0000256|RuleBase:RU366072}.
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DR EMBL; AE000782; AAB90578.1; -; Genomic_DNA.
DR PIR; G69332; G69332.
DR RefSeq; WP_010878166.1; NC_000917.1.
DR AlphaFoldDB; O29594; -.
DR SMR; O29594; -.
DR STRING; 224325.AF_0663; -.
DR PaxDb; 224325-AF_0663; -.
DR EnsemblBacteria; AAB90578; AAB90578; AF_0663.
DR GeneID; 24794263; -.
DR KEGG; afu:AF_0663; -.
DR eggNOG; arCOG02234; Archaea.
DR HOGENOM; CLU_020302_1_0_2; -.
DR OrthoDB; 32867at2157; -.
DR PhylomeDB; O29594; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.3270; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF00037; Fer4; 2.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU366072};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366072};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366072}; Iron {ECO:0000256|RuleBase:RU366072};
KW Iron-sulfur {ECO:0000256|RuleBase:RU366072};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366072};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366072};
KW Reference proteome {ECO:0000313|Proteomes:UP000002199}.
FT DOMAIN 95..124
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 142..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 404 AA; 44360 MW; EC8F1E6453E65B52 CRC64;
MAGEILVIGG GISGLTAAIE AAETGYDVIL LEKNPYLGGR VSQLNKYFPK LCPPFCGLEI
LFKRMKSTPK LKYFTNAEVQ EISGESGNFT VKVKLKPRYV NENCTACGAC KEVCPIEAPD
EYNFGLKKKK AIDLPNIMAM PFQYYIDDKY CNKCGECVSA CKYNAIDLNE EEREMTLNVS
SIIVATGWKP YDATKLDNLG YGKYKNVITN MEMERLASPN GPTGGVIQTM DGKPIETIAF
VQCAGSRDEN HLPYCSAICC LASLKQATYV REQYPDAKIY IFYIDIRAFG RYEDFFAKVK
ADEKIELIKG KVAKVEEVDG KLVVTAEDTL TGVKSKKEVD MVVLATGMQP AIEPIPGLEL
DEYGFVKPKP GIIPVGVAAM PMEVASANET ATAAALKAIQ LARR
//
