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Database: UniProt
Entry: A0A1B7LI22_9FIRM
LinkDB: A0A1B7LI22_9FIRM
Original site: A0A1B7LI22_9FIRM 
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}.
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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
//
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