ID B3R2T6_CUPTR Unreviewed; 313 AA.
AC B3R2T6;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Glyoxylate reductase / 2-ketogluconate reductase (Glycolate reductase) {ECO:0000313|EMBL:CAQ68617.1};
DE EC=1.1.1.215 {ECO:0000313|EMBL:CAQ68617.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:CAQ68617.1};
GN OrderedLocusNames=RALTA_A0635 {ECO:0000313|EMBL:CAQ68617.1};
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:CAQ68617.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ68617.1, 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).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CU633749; CAQ68617.1; -; Genomic_DNA.
DR RefSeq; WP_012351958.1; NC_010528.1.
DR AlphaFoldDB; B3R2T6; -.
DR GeneID; 29761748; -.
DR KEGG; cti:RALTA_A0635; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_4; -.
DR BioCyc; CTAI977880:RALTA_RS03095-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 1.
DR GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:CAQ68617.1}.
FT DOMAIN 44..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..281
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 313 AA; 32680 MW; 67FC1FC85205DD44 CRC64;
MPAPQIVQVG PLAPQTNAIL QQQYGAAALW QQADALAWAR GEGQQVRVVV TSARHGCSAA
LIDALPRLEA IVSFGVGYDA IALDAARARG IQVSNTPDVL NDCVADLAFG LLLDAARGIA
HGDRFVRAGR WPQGGFPLTT RVSGKKLGIV GLGRIGEIVA RRAQGFDMEI AYHNRRPRQG
APWRFEADLK ALAAWADFLV VATVGGPSTA GLVSRDILDA LGPRGILVNV SRGSVVDEAA
LVAALAEGRL GGAGLDVFQD EPNVPPALLA MDHVVLAPHV ASGTHETRAA MTALTLQNLD
AFLAGGKVLT PVL
//
