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Database: UniProt
Entry: A0A1U7EEW9_9LACT
LinkDB: A0A1U7EEW9_9LACT
Original site: A0A1U7EEW9_9LACT 
ID   A0A1U7EEW9_9LACT        Unreviewed;       310 AA.
AC   A0A1U7EEW9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BW721_05200 {ECO:0000313|EMBL:APZ50256.1};
OS   Jeotgalibaca sp. PTS2502.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Jeotgalibaca.
OX   NCBI_TaxID=1903686 {ECO:0000313|EMBL:APZ50256.1, ECO:0000313|Proteomes:UP000187137};
RN   [1] {ECO:0000313|EMBL:APZ50256.1, ECO:0000313|Proteomes:UP000187137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PTS2502 {ECO:0000313|EMBL:APZ50256.1,
RC   ECO:0000313|Proteomes:UP000187137};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP019433; APZ50256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7EEW9; -.
DR   STRING; 1903686.BW721_05200; -.
DR   KEGG; jep:BW721_05200; -.
DR   Proteomes; UP000187137; Chromosome.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187137}.
FT   DOMAIN          19..97
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          98..272
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   310 AA;  34831 MW;  54458546D33DA948 CRC64;
     MTDLKNHQIK ELEDSLAGFE LIRTIPEDKR QLSRIEIVVG WTKELTELWQ QGDLISLKWI
     QAISAGVNSL PLDSLREHGV MLTNASGIHK DTISEHVIGL ILYHARSFNQ IKLNQQNNHW
     DQAVSVQQLE GKTAIIFGIG NIGRRLATLL KAFGVHTIGV NTRGNKVAEV DQTVSQEESN
     RYLEQADYVI NILPQTDETK DFFNSDRFKA MKKGTAFFNV GRGNAVDTEA LLTALDSNQL
     AFAALDVFET EPLEADSPLW QHDRIFITPH VSGMVEHFRD ALFSVVGPNA QAYGENGKPS
     LNMVDYEKRY
//
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