ID A0A1D8Y746_9GAMM Unreviewed; 351 AA.
AC A0A1D8Y746;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:AOX61404.1};
GN ORFNames=BIZ42_03890 {ECO:0000313|EMBL:AOX61404.1};
OS Stenotrophomonas sp. LM091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX61404.1, ECO:0000313|Proteomes:UP000177427};
RN [1] {ECO:0000313|EMBL:AOX61404.1, ECO:0000313|Proteomes:UP000177427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM091 {ECO:0000313|EMBL:AOX61404.1,
RC ECO:0000313|Proteomes:UP000177427};
RA Lefeuvre P.;
RT "Complete genome sequence of a copper-resistant commensal bacteria:
RT Stenotrophomonas sp. strain LM091.";
RL Submitted (SEP-2016) 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; CP017483; AOX61404.1; -; Genomic_DNA.
DR RefSeq; WP_070425599.1; NZ_CP017483.1.
DR AlphaFoldDB; A0A1D8Y746; -.
DR STRING; 1904944.BIZ42_03890; -.
DR KEGG; slm:BIZ42_03890; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000177427; 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 CDD; cd05301; GDH; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 13..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 351 AA; 36937 MW; 53A580ECBCE6DFF6 CRC64;
MADPRPKVWV SQPLFDDVVE QLGQHFDLTM TGDVTRYTPQ GLAEQLAGVD GALITLNERI
GAAEIANAPR LRAIANVGVG YNNLDIDALS TAGILASNTP DVLTETTADL GFALLMATAR
RITESERWLR DGQWGQWSFQ TMLGADIHGS TLGILGMGRI GQGIARRGAH GFGMRVLYHN
RSRLPEATEA EVGAQYVDLD TLLAQVDHLV LVLPYNASSH HIIDAAALAK MKPTATLVNI
ARGGIVDELA LADALAKGRL AAAGLDVFEG EPTVRPELLA LHNIVLTPHI GSASQATRRA
MVQLAVDNLT AALGQGPNAG HPPSAINADA VAAVKTGGAT VGGKKIDDAK R
//
