ID I7KDA9_METBM Unreviewed; 674 AA.
AC I7KDA9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
GN Name=hdrA3 {ECO:0000313|EMBL:CCJ36651.1};
GN OrderedLocusNames=BN140_1728 {ECO:0000313|EMBL:CCJ36651.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ36651.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
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; HE964772; CCJ36651.1; -; Genomic_DNA.
DR RefSeq; WP_014867625.1; NC_018227.2.
DR AlphaFoldDB; I7KDA9; -.
DR STRING; 1201294.BN140_1728; -.
DR GeneID; 27137919; -.
DR KEGG; mbg:BN140_1728; -.
DR PATRIC; fig|1201294.9.peg.1895; -.
DR HOGENOM; CLU_020302_0_0_2; -.
DR BioCyc; MBOU1201294:BN140_RS08635-MONOMER; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000009007; 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; -; 1.
DR Gene3D; 3.30.70.3270; -; 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; PF14697; Fer4_21; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 4.
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 ECO:0000313|EMBL:CCJ36651.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007}.
FT DOMAIN 254..281
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 301..332
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 593..623
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 627..656
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 674 AA; 73330 MW; 71929E402EC875C2 CRC64;
MAEVKKYEEP RIGVFVCHCG TNIAGSIDVK AVMEYARTLP NVIVADDYQY MCSTPGQNKI
AEAIDEQKLT GIVVAACSPR LHEPTFRNAT KMGGLNPFRF EMANIREQNS WVHMHQPEEA
TEKAKDAVRI AVAKAALLED LIPKSVPVEK AAMVVGGGVG GMQAALDLAN AGIKTYLVEK
TPTIGGRMSQ LDKTFPTLDC SQCILTPKMV DVYRNENIEL LTYTEVEAVE GYIGNFDVTL
RKKARGVLTP DEATARGIIG GGCTGCGDCE SVCPVIKPNP FELGMAPRKA IYIYHPQVSP
LIYTVDFDAC VKCGLCVEAC GEERKAIDLD AKDELMTVKV GTVILATGYD IFPIEKKFEW
GYKNYDNVIT SLEFERLICA SGPTGGHLIR PSDGVTPKKV AFVLCAGSRD NTGVGKPYCS
RFCCMYSLKH AHQIIEKIPG AVPYIFYMDI RSFGKMYEEF YYRIQNEGAK FIRGRVANIL
EDPATKNLHV YAEDTLLGRP IDMEVDMVVL AAAIEPSAET EKTRRLFGVS CSQDGWLLEA
HPKLNPCGTT TAGVYLAGVC QGPKDIPDTV AQAEGAASAA SIPIHRGEVE LEPYFAVCLE
DKCAGCGLCI NQCPYQALSL VEKEGRTVMQ VTEAKCKGCG TCGGFCPGGA IWMQHFATPQ
IIAQIDAFLL GGEQ
//
