ID A0A1W2BNR5_9FLAO Unreviewed; 316 AA.
AC A0A1W2BNR5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SMC74484.1};
GN ORFNames=SAMN05660703_2570 {ECO:0000313|EMBL:SMC74484.1};
OS Cellulophaga tyrosinoxydans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=504486 {ECO:0000313|EMBL:SMC74484.1, ECO:0000313|Proteomes:UP000192360};
RN [1] {ECO:0000313|EMBL:SMC74484.1, ECO:0000313|Proteomes:UP000192360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21164 {ECO:0000313|EMBL:SMC74484.1,
RC ECO:0000313|Proteomes:UP000192360};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWXO01000004; SMC74484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2BNR5; -.
DR STRING; 504486.SAMN05660703_2570; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000192360; 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; cd05303; PGDH_2; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000192360}.
FT DOMAIN 6..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 135..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 316 AA; 34554 MW; F3C988649312C9AE CRC64;
MRILANDGIS QAGVDTLKSN GFEILTVNVA QEQLVTYINK HNIEALLVRS ATKVQKDIID
QCPSLKLIGR GGVGMDNIDV EYAIEKGIHV INTPEASSES VAELVFAHLY GGVRFLYDSN
RTMPLDGDSR FKELKKGYSG GIELRGKTLG IIGFGKIGQA TAKIALGVGM KVIYHDSELE
KSTISLKFFD GQKVDFNLIN STKDEVLKKS DFISLHVPKQ KNYILDKDDF EIMKDGVAII
NTARGGVLDE VALVNALETG KVSFAGLDVF ESEPKPEIRI LMHPDISLTP HIGAATQEAQ
DRIGIELANK ITKLLK
//
