ID A0A135VFA1_9ARCH Unreviewed; 654 AA.
AC A0A135VFA1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AM324_08760 {ECO:0000313|EMBL:KXH71374.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-83.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH71374.1, ECO:0000313|Proteomes:UP000070043};
RN [1] {ECO:0000313|EMBL:KXH71374.1, ECO:0000313|Proteomes:UP000070043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH71374.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
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:KXH71374.1}.
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DR EMBL; LRSK01000230; KXH71374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VFA1; -.
DR Proteomes; UP000070043; 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 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 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 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; 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}.
FT DOMAIN 455..484
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 485..513
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 654 AA; 71787 MW; 02B48A988AB892B6 CRC64;
MKKLFLCTCN GTLNKLLDFT RIGKEAKAIY DVVEVADNLC LEEGLAELEK GLSGDDRLVI
GACSSQIIGV PMKQRIKNDL VAFVPLREQV GWVHLEEGES ATNKAIVLLS DAAVQLDYME
SQAEFTENMV GRVLVIGGGI AGLKAASDLH RLGVEVTLLE PFKLDKHHYL QTSVFMSDAD
TLRSEIQEIQ KTILDVERIR GEIREVRGQL GSYEVTINGA KDGSMTQEFG AIIIASGNQQ
SLPSSAKKMR YGKSERVVTL DSLISNSKKK RAKDRSTILV AVDFDAPMSS VEGSHLLRTT
RDLAARGNTI IVVYSDIQTE DENLYREARD SGVIFIRGRV TRIKENDKGL SCRIENTLES
MQRDVIADRV AIPRLIGPTI ETTQIAEKLG VECDDSGFIR TRYSKMKPVQ TSRRGIFVAG
GAKMPMSLSD AMASAQNAVL EAFKIVRSPL VRSGWIPVID DEECDVCKAC LDACPNDALR
LMDGRIVHIP AHCEFCGICV SACPTRAIEF QSHSKESWFA RFEAIAATHK RLEGKKPFSL
VFACSECANA SIDQAGFVGK QYGTGSYVIQ FPCAGMVSPI EILKGLVVGA NRVIVAHCPP
GGCHHQTGDH LSELIVSLTR DMLREIGQNP DRVRATYMMA AMPDKMQKEV PVRG
//
