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Database: UniProt
Entry: A0A151B8J5_9ARCH
LinkDB: A0A151B8J5_9ARCH
Original site: A0A151B8J5_9ARCH 
ID   A0A151B8J5_9ARCH        Unreviewed;       543 AA.
AC   A0A151B8J5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE            EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
DE   Flags: Fragment;
GN   ORFNames=AYL30_008000 {ECO:0000313|EMBL:KYH36261.1};
OS   Candidatus Hecatellales archaeon B24.
OC   Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia;
OC   Candidatus Hecatellales.
OX   NCBI_TaxID=1779369 {ECO:0000313|EMBL:KYH36261.1, ECO:0000313|Proteomes:UP000075493};
RN   [1] {ECO:0000313|EMBL:KYH36261.1, ECO:0000313|Proteomes:UP000075493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B25 {ECO:0000313|EMBL:KYH36261.1};
RA   He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT   "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT   phylum Bathyarchaeota widespread in marine sediments.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYH36261.1}.
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DR   EMBL; LUCC01000063; KYH36261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151B8J5; -.
DR   STRING; 1779369.AYL30_008000; -.
DR   PATRIC; fig|1779369.3.peg.984; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000075493; Unassembled WGS sequence.
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; -; 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   InterPro; IPR003813; MvhD/FlpD.
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; PF12838; Fer4_7; 1.
DR   Pfam; PF02662; FlpD; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
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}.
FT   DOMAIN          29..63
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          324..353
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          354..382
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KYH36261.1"
SQ   SEQUENCE   543 AA;  59777 MW;  0F7A973CA204DDA8 CRC64;
     CPVKLPNEFD YGLSQRKAIY LPFEEAVPKR YLIDPENCLK LTKNVCEVCK KVCKADAIDF
     EMKEETVKVT ADAIIIATGI EAFDARLKEN YGYGRYKNVV ISPQIERMIV PTGPTKGKII
     RPGDGKEPKR FAFILCVGSR DEQVGNLYCS RVCCMYAIKE ASFLKRRDPS RSIYLFYTDI
     RAFGKGFEEY YNEAQKVGVK FIRGRVAEIK ENPETGNLTV KAENTLTGEI VELEFDLIVL
     AVGLVANPGS TVIKECLKLP VDSYGFFTEA HPKLKPVETI LDGVFICGCA AGPKDIPDSV
     AQAGAAAAKT MNLLAREAVE TDPIRVYVDD ALCDGCGECL EACPLKAISL KESKAAVNPL
     LCKGCGSCVG SCSKGALNLA NYTDAQLEAM IKAAVERSFA KPLLLVFIDD WAAYHVSDFA
     GLNRLSYPPN LLFIRVPSTC RVHHRLILKA LSMGVDGVFL ADTEFASAPY IDESMKETDK
     AVGKAREALA KLGLDPERVT FLRYVSTQAP RFAMTMRKFA ESMKGKTLSD EDRVKIKEFL
     GGI
//
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