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Database: UniProt
Entry: Q59516
LinkDB: Q59516
Original site: Q59516 
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   13-FEB-2019, entry version 119.
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   Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 /
OS   NCIMB 9133 / AM1) (Methylorubrum extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
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
RT   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.,
RA   Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C.,
RA   Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S.,
RA   Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G.,
RA   Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z.,
RA   Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J.,
RA   Medigue C., Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to
RT   investigate microbial metabolism of C1 compounds from natural and
RT   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
RT   the facultative methylotroph Methylobacterium extorquens AM1.";
RL   J. Bacteriol. 173:7228-7232(1991).
CC   -!- FUNCTION: Plays a central role in assimilation of carbon. It
CC       converts hydroxypyruvate to glycerate as a key step in the serine
CC       cycle, and may also play an important role in C2 reactions, by
CC       interconverting 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;
CC         EC=1.1.1.29;
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via
CC       serine 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}.
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   ProteinModelPortal; Q59516; -.
DR   SMR; Q59516; -.
DR   STRING; 272630.MexAM1_META1p1727; -.
DR   EnsemblBacteria; ACS39571; ACS39571; MexAM1_META1p1727.
DR   KEGG; mea:Mex_1p1727; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00018; -.
DR   OMA; PHIAWAY; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; MetaCyc:MONOMER-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   Complete proteome; Cytoplasm; Direct protein sequencing; NAD; NADP;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    314       Glycerate dehydrogenase.
FT                                /FTId=PRO_0000075943.
FT   NP_BIND     157    158       NAD. {ECO:0000250}.
FT   NP_BIND     228    230       NAD. {ECO:0000250}.
FT   NP_BIND     280    283       NAD. {ECO:0000250}.
FT   ACT_SITE    230    230       {ECO:0000250}.
FT   ACT_SITE    259    259       {ECO:0000250}.
FT   ACT_SITE    280    280       Proton donor. {ECO:0000250}.
FT   BINDING      74     74       NAD. {ECO:0000250}.
FT   BINDING     254    254       NAD. {ECO:0000250}.
FT   CONFLICT     22     22       F -> N (in Ref. 4; AA sequence).
FT                                {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
//
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