ID B3R8G5_CUPTR Unreviewed; 309 AA.
AC B3R8G5;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase 6-phosphogluconate dehydrogenase hydroxyacid dehydrogenase {ECO:0000313|EMBL:CAQ71321.1};
DE EC=1.1.-.- {ECO:0000313|EMBL:CAQ71321.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:CAQ71321.1};
GN OrderedLocusNames=RALTA_B0703 {ECO:0000313|EMBL:CAQ71321.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ71321.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ71321.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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DR EMBL; CU633750; CAQ71321.1; -; Genomic_DNA.
DR RefSeq; WP_012355542.1; NC_010530.1.
DR AlphaFoldDB; B3R8G5; -.
DR GeneID; 29764355; -.
DR KEGG; cti:RALTA_B0703; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_4; -.
DR BioCyc; CTAI977880:RALTA_RS19145-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 2.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12164; GDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAQ71321.1}.
FT DOMAIN 101..274
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 309 AA; 33230 MW; 308B112DACB1BF9D CRC64;
MAILVHLPSF MAVPITALLR EAAPDITVWN GREAAVADEV EAIIAWGLKP GVVPAYPNLR
LVCAATAGVD KLLAAPDLPA HIPVTRIVDP GQQAGIARFV LAMALRHTRS LGLYAEQQRR
GEWKRHAGRD AAQCRVGVLG LGEIGSEVAR MFVAIGYPVS GWSRAAKHLP GVTDFTGDDG
LDAMLAQSDI LVCTLPLTPR TEGLLDRRTL SRLPRGAYLI NVGRGEHVVE PDLVALIDEG
HLAGAALDVF AKEPPAADDP VWNHPRIEAT PHIAADPSYP LVARQCLDNL RRAREGRALL
NLVDRQAGY
//
