ID A0A2V2NFW8_9EURY Unreviewed; 430 AA.
AC A0A2V2NFW8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
GN ORFNames=DK846_02340 {ECO:0000313|EMBL:PWR74501.1};
OS Methanospirillum lacunae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=668570 {ECO:0000313|EMBL:PWR74501.1, ECO:0000313|Proteomes:UP000245657};
RN [1] {ECO:0000313|EMBL:PWR74501.1, ECO:0000313|Proteomes:UP000245657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ki8-1 {ECO:0000313|EMBL:PWR74501.1,
RC ECO:0000313|Proteomes:UP000245657};
RA Dueholm M.S., Nielsen P.H., Bakmann L.F., Otzen D.E.;
RT "Draft genome of Methanospirillum lacunae Ki8-1.";
RL Submitted (MAY-2018) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PWR74501.1}.
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DR EMBL; QGMY01000002; PWR74501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2NFW8; -.
DR OrthoDB; 32867at2157; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000245657; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 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; PF13187; Fer4_9; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
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:UP000245657}.
FT DOMAIN 95..125
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 141..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 430 AA; 46967 MW; 272E290942733CD6 CRC64;
MSEVVVIGGG IAGITAALDL ANHNIHVHLI EREPTIGGHM AMLDKTFPTN DCSMCILSPK
MVDAARHPKI SLHTCTEVTR IEGDVGDFTV HVTRHPRYIK ESECTGCDDC VAICPVEVYN
KFDAGLGVRK AIYKSHPQVV PNIVIRDAEH CINCGLCYSV CGKKAILRDH EDGEEQAFIK
ASAVIVSTGY EVFDATKKPA YHYLRIPDVI SSIEFERMIN ASGPTSGALK KRSDGTKPKK
IVFIQCVGSR DCAIGSPSCS AVCCMYAIKN ALLIKEKSPD TEVTVLYMDI RAYGKGYEEF
YERAIRAGVR FVRGLPGDLY QNNAHIRVHV ENTENQEIIK IDADLVVLSV GIRPQTDAAE
IAKRLNISLD DTGFYASVDQ KSEHISAIRP GIFLAGTCRE PMDIPDTVAE GGAAAMRAVI
RCMKGEHAAL
//
