ID A0A1B7LI22_9FIRM Unreviewed; 413 AA.
AC A0A1B7LI22;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 02-APR-2025, entry version 33.
DE SubName: Full=Heterodisulfide reductase subunit A {ECO:0000313|EMBL:OAT85942.1};
GN ORFNames=A6M21_17055 {ECO:0000313|EMBL:OAT85942.1};
OS Desulfotomaculum copahuensis.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Desulfotomaculaceae; Desulfotomaculum.
OX NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT85942.1, ECO:0000313|Proteomes:UP000078532};
RN [1] {ECO:0000313|EMBL:OAT85942.1, ECO:0000313|Proteomes:UP000078532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMa1 {ECO:0000313|EMBL:OAT85942.1,
RC ECO:0000313|Proteomes:UP000078532};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the HdrA family.
CC {ECO:0000256|ARBA:ARBA00006561}.
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:OAT85942.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LYVF01000046; OAT85942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7LI22; -.
DR STRING; 1838280.A6M21_17055; -.
DR Proteomes; UP000078532; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; PF00037; Fer4; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000078532}.
FT DOMAIN 96..124
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 142..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 413 AA; 45631 MW; E0A5B7508C71CB04 CRC64;
MEKSILVVGG GISGITTALE AAEAGREVFL VEKNPYLGGR VAQLNQYFPK LCPPNCGLEI
NFKRLKQNPR IRFFTMAEVE KISGQEGDFE VTVRLNPRYV NQNCTACGKC AEVCPLERPN
AFNYGLDKTK AIYLPHVFAF PMKYVIDKQV CDSCGKCVEA CQYNAIELDM EPKTINLKVG
AIVWATGWQP YDATKLSYYG FGRYENVITN VMMERLAAGN GPTGGKIVRP SDGKEINSIA
FVQCAGSRDE NHLHCCSNVC CLATLKQATY VRKQYPGAKI SIFFIDIRAR GKYEDFFVKV
QNEDDITLIK GKAGEIKEDA DKNLTVIAED QLNQNLLEEK FDLVVLATGM APGTREDKIP
LDVCYDEDGF FDTDPQTPGI YGAGCVKQPL DVASAVRDAT AAALKAIQST VRR
//