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
//