ID   O29030_ARCFU            Unreviewed;       769 AA.
AC   O29030;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 140.
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_1238 {ECO:0000313|EMBL:AAB90008.1};
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:AAB90008.1, ECO:0000313|Proteomes:UP000002199};
RN   [1] {ECO:0000313|EMBL:AAB90008.1, 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; AAB90008.1; -; Genomic_DNA.
DR   PIR; E69404; E69404.
DR   RefSeq; WP_010878733.1; NC_000917.1.
DR   AlphaFoldDB; O29030; -.
DR   SMR; O29030; -.
DR   STRING; 224325.AF_1238; -.
DR   PaxDb; 224325-AF_1238; -.
DR   EnsemblBacteria; AAB90008; AAB90008; AF_1238.
DR   GeneID; 24794841; -.
DR   KEGG; afu:AF_1238; -.
DR   eggNOG; arCOG02235; Archaea.
DR   eggNOG; arCOG02476; Archaea.
DR   HOGENOM; CLU_020302_0_0_2; -.
DR   OrthoDB; 32867at2157; -.
DR   PhylomeDB; O29030; -.
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; 3.30.70.20; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039650; HdrA-like.
DR   InterPro; IPR003813; MvhD/FlpD.
DR   NCBIfam; NF040770; hetero_SS_HdrA2; 1.
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; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF02662; FlpD; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
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          233..264
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          282..311
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          567..596
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          597..624
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   769 AA;  84765 MW;  798037D73522FA83 CRC64;
     MRIGVFVCHC GLNIARVVDV KELVEYAKTI DGVVHAEDID YACSDSGQEE ILNAIKEKNL
     DAFVVAACSP KLHEPTFRRV AIRAGLNPYM VEIANIREQC SWVHQAKPKA ALAKAKDLIR
     MAVAKARTNR PLERRKAEIE RSVAVIGGGV AGIEAALTLA DSGIKVYLIE KNPTIGGHMA
     TLNEVFPTND CSICILAPKM SDVWNHENIE VITNAEIDEI NGSVGNFRIK VIKHPRYVDE
     SKCKGCIDDC SSVCPVEIPN EFDYGIGVRK AIYIPIPQST PLYAAIDWEH CIGCRLCEKA
     CQPKAVDFSQ QPETLEIKAG AIIVATGYKI FDARRKTEYG YGRFKNVITT IELERLLSAS
     GPTMGRLLRP SDSTVPKRIA FIQCVGSRDE KTNKYCSRVC CMVSLKNAYA IKERYHDAEI
     TIFYIDIRAF GRMYEEFYRR VQEAGVRFIR GKVGEIIENE NGNLIVSYES TLEGEVREEE
     FDLVVLSIGI EGNRDVATKL GLGIGEDGFF EVAHPKLRPA ETNVKGIFLA GCASGPRDIQ
     DSVASAGLAA AKAAQLVLTG ETEFDPYNAY VDEEKCIGCR ICEKVCEFNA VTVDRKAKIN
     PNACAMCGIC VAACPADAID MGFFSDEGIK AMIDALGEEK NADPLALAFA CWYCSYGAAD
     LAGTTKVQYE PNVRIIRVLC SGRVDPEWVL RALARGIDGV IIAGCRLGEC HFKYGNYKAK
     DRFEALKEAL KEVGIEPERV RCIWHSAGEA EGIANDFNEF VEELKKLKS
//