ID   A0A495PYQ3_9FLAO        Unreviewed;       315 AA.
AC   A0A495PYQ3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   22-FEB-2023, entry version 9.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:RKS55751.1};
GN   ORFNames=BC962_0721 {ECO:0000313|EMBL:RKS55751.1};
OS   Gillisia mitskevichiae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gillisia.
OX   NCBI_TaxID=270921 {ECO:0000313|EMBL:RKS55751.1, ECO:0000313|Proteomes:UP000276282};
RN   [1] {ECO:0000313|EMBL:RKS55751.1, ECO:0000313|Proteomes:UP000276282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19839 {ECO:0000313|EMBL:RKS55751.1,
RC   ECO:0000313|Proteomes:UP000276282};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:RKS55751.1}.
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DR   EMBL; RBLG01000001; RKS55751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495PYQ3; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000276282; Unassembled WGS sequence.
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   CDD; cd12179; 2-Hacid_dh_14; 1.
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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR   PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          10..309
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          105..289
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   315 AA;  35365 MW;  41FB760CFA9CBF5C CRC64;
     MIVLHADSNN PLLIKELQKV GYHNVEAYDV CKEDILANQH LFDGIIIRSR FKIDKDFIDR
     APNLKFIARV GAGLESIDVE YAKESGIELF AAPEGNSNAV GEHALGMLLS LLNKLTKANR
     EVHQGYWHRE DNRGIELDGK TVGIIGYGNM GKAFAKKLRG FDVKVLCYDI LKGVGDENAT
     QVSLEELQNT AEVLSLHTPW TQQTNKMVNT NFINKFKNPF WFINTARGKS VITADLVLGL
     IEGKILGAGL DVLEYEKDSF EHLFQDHQIP PDLKELMFFE NVILSPHVAG WTEESHRKLA
     STIAYKIIDK FGEAI
//