DHGY_METEA
ID DHGY_METEA Reviewed; 314 AA.
AC Q59516; C5B107;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glycerate dehydrogenase;
DE Short=GDH;
DE EC=1.1.1.29;
DE AltName: Full=Glyoxylate reductase;
DE AltName: Full=Hydroxypyruvate dehydrogenase;
DE AltName: Full=NADH-dependent hydroxypyruvate reductase;
DE Short=HPR;
DE Short=HPR-A;
GN Name=hprA; OrderedLocusNames=MexAM1_META1p1727;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8144463; DOI=10.1128/jb.176.7.1957-1968.1994;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Genetics of the serine cycle in Methylobacterium extorquens AM1:
RT identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA.";
RL J. Bacteriol. 176:1957-1968(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=1729225; DOI=10.1128/jb.174.1.71-77.1992;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Cloning, mutagenesis, and physiological effect of a hydroxypyruvate
RT reductase gene from Methylobacterium extorquens AM1.";
RL J. Bacteriol. 174:71-77(1992).
RN [4]
RP PROTEIN SEQUENCE OF 3-24, AND CHARACTERIZATION.
RX PubMed=1657886; DOI=10.1128/jb.173.22.7228-7232.1991;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Purification and characterization of hydroxypyruvate reductase from the
RT facultative methylotroph Methylobacterium extorquens AM1.";
RL J. Bacteriol. 173:7228-7232(1991).
CC -!- FUNCTION: Plays a central role in assimilation of carbon. It converts
CC hydroxypyruvate to glycerate as a key step in the serine cycle, and may
CC also play an important role in C2 reactions, by interconverting
CC glyoxylate and glycolate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.29;
CC -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine
CC pathway.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Uses both NAD and NADP.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L27235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP001510; ACS39571.1; -; Genomic_DNA.
DR EMBL; M81443; AAA25378.1; -; Genomic_DNA.
DR PIR; A44921; A44921.
DR RefSeq; WP_003597638.1; NC_012808.1.
DR AlphaFoldDB; Q59516; -.
DR SMR; Q59516; -.
DR STRING; 272630.MexAM1_META1p1727; -.
DR EnsemblBacteria; ACS39571; ACS39571; MexAM1_META1p1727.
DR KEGG; mea:Mex_1p1727; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_5; -.
DR OMA; PHIAWAY; -.
DR OrthoDB; 1638924at2; -.
DR BioCyc; MetaCyc:MON-3821; -.
DR UniPathway; UPA00927; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..314
FT /note="Glycerate dehydrogenase"
FT /id="PRO_0000075943"
FT ACT_SITE 230
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 157..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228..230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="F -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34269 MW; B2711E02520A5144 CRC64;
MTKKVVFLDR ESLDATVREF NFPHEYKEYE STWTPEEIVE RLQGAEIAMI NKVPMRADTL
KQLPDLKLIA VAATGTDVVD KAAAKAQGIT VVNIRNYAFN TVPEHVVGLM FALRRAIVPY
ANSVRRGDWN KSKQFCYFDY PIYDIAGSTL GIIGYGALGK SIAKRAEALG MKVLAFDVFP
QDGLVDLETI LTQSDVITLH VPLTPDTKNM IGAEQLKKMK RSAILINTAR GGLVDEAALL
QALKDGTIGG AGFDVVAQEP PKDGNILCDA DLPNLIVTPH VAWASKEAMQ ILADQLVDNV
EAFVAGKPQN VVEA
