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Database: UniProt
Entry: I3VXQ1_THESW
LinkDB: I3VXQ1_THESW
Original site: I3VXQ1_THESW 
ID   I3VXQ1_THESW            Unreviewed;       454 AA.
AC   I3VXQ1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:AFK87296.1};
GN   OrderedLocusNames=Tsac_2292 {ECO:0000313|EMBL:AFK87296.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK87296.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK87296.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
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DR   EMBL; CP003184; AFK87296.1; -; Genomic_DNA.
DR   RefSeq; WP_014759133.1; NC_017992.1.
DR   AlphaFoldDB; I3VXQ1; -.
DR   STRING; 1094508.Tsac_2292; -.
DR   KEGG; tsh:Tsac_2292; -.
DR   PATRIC; fig|1094508.3.peg.2321; -.
DR   eggNOG; COG0644; Bacteria.
DR   BioCyc; TSAC1094508:GLMA-2325-MONOMER; -.
DR   Proteomes; UP000006178; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   454 AA;  50592 MW;  D21E708D5BDBCEBB CRC64;
     MDYYIYKNNK IPILDDKYDV IIVGGGTAGS IAAIASAREG AKTLIIEKYG FLGGSSTAAQ
     VTPMMHVNIS GNPASSIDKE IRRRLINYGY GAKDSSGNDG WFNPEMMKFV LEEMLLEYNG
     LILYDTFFLG SIVEDYTIKG VLVHNKSGIS AIFGKVVIDC TGDADVAFSA GVPCFIGDER
     TSKNQAISLR FMVGNIDLIK LQSFLRDLGQ NWGLDYPLIE TAMVWNSNFP LESIFKKGLD
     DKIINYEDGV YFQAFSIPGM SGVMSFNCPE IPAIKDVLNA KEISYSYQKG REMIQRLYKF
     LKKYIPGFEE SYILSVAPMI GIRESRRIKG KYILNIDDYN NRSKFNDAIA KTAYPVDVHG
     MKTELKILPI ENNEYFEIPF RCLIPLNIEG LLVAGRCISS TFIAQSSIRI QPTCRATGEA
     AGIAAAYSIQ KGIKVSKIDG CEIRKIMRDY GYDI
//
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