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Database: UniProt
Entry: K8EL61_9FIRM
LinkDB: K8EL61_9FIRM
Original site: K8EL61_9FIRM 
ID   K8EL61_9FIRM            Unreviewed;       335 AA.
AC   K8EL61;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Putative tartrate dehydrogenase {ECO:0000313|EMBL:CCO09256.1};
GN   Name=yeaU {ECO:0000313|EMBL:CCO09256.1};
GN   ORFNames=DESHY_70042 {ECO:0000313|EMBL:CCO09256.1};
OS   Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO09256.1, ECO:0000313|Proteomes:UP000009315};
RN   [1] {ECO:0000313|EMBL:CCO09256.1, ECO:0000313|Proteomes:UP000009315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX   PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA   Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA   Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT   "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT   hydrothermale Lam5(T).";
RL   Genome Announc. 1:e00114-e00112(2013).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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:CCO09256.1}.
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DR   EMBL; CAOS01000014; CCO09256.1; -; Genomic_DNA.
DR   RefSeq; WP_008413184.1; NZ_FQXF01000010.1.
DR   AlphaFoldDB; K8EL61; -.
DR   STRING; 1121428.DESHY_70042; -.
DR   eggNOG; COG0473; Bacteria.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000009315; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009315}.
FT   DOMAIN          3..327
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   335 AA;  36242 MW;  E4D82E66BD8185FC CRC64;
     MYKVTLIPGD GIGPEITAAA RQVIEATGVN IRWEVVEAGA AALDRYGKPL PDHVLDAIRR
     NKVALKGPVT TPVGQGFRSV NVTLRQELDL FANLRPARNI PNVPSRYQGV DLLVVRENTE
     DLYAGVEHRV GKDAAESIKI ITREASRRIA RFAFETARRQ GRKKVTAVHK ANIMKLSDGL
     FLESVRSVAE TYPDIAYEEM IVDAMCMKLV QEPENYDVLV LPNLYGDIVS DLCAGLVGGL
     GVAPGANIGL DCAVFEAVHG SAPQIAGQNI ANPLAVILSG VMMLRHLGEQ QCAALIEEAV
     REVLAEGRHL TADLGGSATT GQMAEAISRR IYDKR
//
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