ID A0A0C4Y2V0_9BURK Unreviewed; 317 AA.
AC A0A0C4Y2V0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AJG19507.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:AJG19507.1};
GN ORFNames=RR42_m2115 {ECO:0000313|EMBL:AJG19507.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG19507.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG19507.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG19507.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010536; AJG19507.1; -; Genomic_DNA.
DR RefSeq; WP_043346376.1; NZ_CP010536.1.
DR AlphaFoldDB; A0A0C4Y2V0; -.
DR STRING; 68895.RR42_m2115; -.
DR KEGG; cbw:RR42_m2115; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000031843; Chromosome main.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12156; HPPR; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:AJG19507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT DOMAIN 38..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..284
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 33864 MW; 3D7D99B4B8A88397 CRC64;
MKPQILQLNP ILIPAANEEL AALYEVHKYF EIEDQAVWLA QHGPSIQAVI TGGHTGISRA
MLEQLPALKV VAVNGVGTDA VDLAYCRERG LPVTATLGAL TEDVADLAIG LLIAACRNIC
AGDRFVRDGQ WERFPQPSAI PLARRFSGMR VGIVGMGRVG RAVATRAAAF GCPIRYTDLQ
RMNDLPHEFV SDLVDLARDS DALVLCAAAD KAEGIVNAEV LDALGPRGFL VNVARGRLVN
EVDLAQAIEA GSIAGAGLDV FVDEPRVPLA LRQSDRTTLQ AHRASATWET RAAMIRMVLD
SVADGLAGKR PSMSLTT
//
