ID A0A1X7L6A7_9SPHI Unreviewed; 313 AA.
AC A0A1X7L6A7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SMG49290.1};
GN ORFNames=SAMN05660862_3644 {ECO:0000313|EMBL:SMG49290.1};
OS Sphingobacterium psychroaquaticum.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=561061 {ECO:0000313|EMBL:SMG49290.1, ECO:0000313|Proteomes:UP000192980};
RN [1] {ECO:0000313|EMBL:SMG49290.1, ECO:0000313|Proteomes:UP000192980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22418 {ECO:0000313|EMBL:SMG49290.1,
RC ECO:0000313|Proteomes:UP000192980};
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; FXAU01000008; SMG49290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7L6A7; -.
DR STRING; 561061.SAMN05660862_3644; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000192980; 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 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:UP000192980}.
FT DOMAIN 5..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 313 AA; 35038 MW; ACA3771B84678D97 CRC64;
MKTQILIVDD IHEILLEKLK SAGLAYDYQP NIDREGAAAI ISNYSGLIIR SKFQVDRDFI
DLGTNLQFIG RAGAGMDNID EHYATSKGIV LIPANEGNRD AVGEHMIGML LSLMNNLNRA
HKEITEKGQW RREENRGHEL KGKTVALIGY GHNGQAMAKK LAGFEVNVIA YDKYKTGFSD
NYAREVSMEE VVKQADILSF HIPLTTETKG LVDDEYLFHF RKPIFFLMGA RGGIVQVPAV
LKALNSKKII AAAFDVLPIE KFPSLGEQEW FHDLSSRDNV LLSPHVAGWT YESYYKLSDV
LAEKIIALEH TAN
//
