ID   S0KJ91_9ENTE            Unreviewed;       320 AA.
AC   S0KJ91;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:EOT40178.1};
GN   ORFNames=OMK_02030 {ECO:0000313|EMBL:EOT40178.1};
OS   Enterococcus dispar ATCC 51266.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT40178.1, ECO:0000313|Proteomes:UP000014127};
RN   [1] {ECO:0000313|EMBL:EOT40178.1, ECO:0000313|Proteomes:UP000014127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT40178.1,
RC   ECO:0000313|Proteomes:UP000014127};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT   assembly).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       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:EOT40178.1}.
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DR   EMBL; AHYR01000009; EOT40178.1; -; Genomic_DNA.
DR   RefSeq; WP_016173169.1; NZ_KE136354.1.
DR   AlphaFoldDB; S0KJ91; -.
DR   STRING; 44009.RV01_GL001444; -.
DR   PATRIC; fig|1139219.3.peg.1972; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000014127; 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; cd12178; 2-Hacid_dh_13; 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; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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:UP000014127}.
FT   DOMAIN          5..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   320 AA;  34548 MW;  68B00AB212294C37 CRC64;
     MTQIYISAQI PQKGVQLLKE NGVTFEMYTG KDVIDQATLQ QKVPEVEVLI TPLSTTVDAA
     IIDAAPKLKL IANFGAGFNN IATDYAKEKG IFVTNTPFVS TDATAELTAG LIISLSRRIV
     AGDHLMRTTG FSGWAPLFFL GHELKDKTLG IIGMGQIGQG VATRLKAFGM KIIYSQRHQL
     PKEVEETLGA TYLTQAEVLA QADIISLHTP LTNGTYHLID QTAFAQMKPG AFLVNASRGP
     IVSEADLITA LQTEKIAGAA LDVYEFEPKV SDTLKQMPQV ILTPHIGNAT VEARDAMAVI
     VANNALAILQ NKKPDYIVNL
//