GenomeNet

Database: UniProt
Entry: Q91Z53
LinkDB: Q91Z53
Original site: Q91Z53 
ID   GRHPR_MOUSE             Reviewed;         328 AA.
AC   Q91Z53;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-FEB-2019, entry version 137.
DE   RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=Grhpr; Synonyms=Glxr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvEv; TISSUE=Liver;
RA   Cramer S.D.;
RT   "Identification of the mouse GRHPR cDNA from liver.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 44-58 AND 303-318, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate
CC       reductase and D-glycerate dehydrogenase enzymatic activities.
CC       Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate
CC       oxidizes D-glycerate to hydroxypyruvate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.79;
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=1.1.1.81;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.81;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AY113690; AAM52985.1; -; mRNA.
DR   EMBL; BC010194; AAH10194.1; -; mRNA.
DR   CCDS; CCDS18128.1; -.
DR   RefSeq; NP_525028.1; NM_080289.2.
DR   UniGene; Mm.196574; -.
DR   ProteinModelPortal; Q91Z53; -.
DR   SMR; Q91Z53; -.
DR   IntAct; Q91Z53; 4.
DR   MINT; Q91Z53; -.
DR   STRING; 10090.ENSMUSP00000047218; -.
DR   iPTMnet; Q91Z53; -.
DR   PhosphoSitePlus; Q91Z53; -.
DR   SwissPalm; Q91Z53; -.
DR   REPRODUCTION-2DPAGE; Q91Z53; -.
DR   EPD; Q91Z53; -.
DR   jPOST; Q91Z53; -.
DR   MaxQB; Q91Z53; -.
DR   PaxDb; Q91Z53; -.
DR   PRIDE; Q91Z53; -.
DR   Ensembl; ENSMUST00000045078; ENSMUSP00000047218; ENSMUSG00000035637.
DR   GeneID; 76238; -.
DR   KEGG; mmu:76238; -.
DR   UCSC; uc008ssb.1; mouse.
DR   CTD; 9380; -.
DR   MGI; MGI:1923488; Grhpr.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; COG1052; LUCA.
DR   GeneTree; ENSGT00940000158578; -.
DR   HOGENOM; HOG000136700; -.
DR   HOVERGEN; HBG051838; -.
DR   InParanoid; Q91Z53; -.
DR   KO; K00049; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 1378766at2759; -.
DR   PhylomeDB; Q91Z53; -.
DR   TreeFam; TF324791; -.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:Q91Z53; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000035637; Expressed in 290 organ(s), highest expression level in liver.
DR   ExpressionAtlas; Q91Z53; baseline and differential.
DR   Genevisible; Q91Z53; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
DR   GO; GO:0008465; F:glycerate dehydrogenase activity; ISO:MGI.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; ISO:MGI.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; ISO:MGI.
DR   GO; GO:0051287; F:NAD binding; ISO:MGI.
DR   GO; GO:0050661; F:NADP binding; ISO:MGI.
DR   GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0043648; P:dicarboxylic acid metabolic process; ISO:MGI.
DR   GO; GO:0007588; P:excretion; ISO:MGI.
DR   GO; GO:0046487; P:glyoxylate metabolic process; ISO:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
DR   GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1    328       Glyoxylate reductase/hydroxypyruvate
FT                                reductase.
FT                                /FTId=PRO_0000075945.
FT   NP_BIND     162    164       NADP. {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   NP_BIND     185    188       NADP. {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   REGION       83     84       Substrate binding.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   REGION      293    296       Substrate binding.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   ACT_SITE    293    293       Proton donor.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   BINDING     217    217       NADP. {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   BINDING     243    243       NADP; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   BINDING     245    245       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   BINDING     269    269       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   BINDING     295    295       NADP; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   SITE        274    274       Raises pKa of active site His.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   MOD_RES      36     36       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
FT   MOD_RES     298    298       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UBQ7}.
SQ   SEQUENCE   328 AA;  35329 MW;  BDEC1ADEC1E18153 CRC64;
     MKPARLMKVF VTGPLPAEGR AALAQAADCE VEQWNSDDPI PRKDLEQGVV GAHGLLCRLS
     DRVDKKLLDA AGANLRVIST LSVGVDHLAL DEIKKRGIRV GYTPGVLTDA TAELAVSLLL
     TTCRRLPEAI EEVKNGGWSS WSPLWMCGYG LSQSTVGIVG LGRIGQAIAR RLKPFGVQRF
     LYTGRQPRPQ EAAEFQAEFV PIAQLAAESD FIVVSCSLTP DTMGLCSKDF FQKMKNTAIF
     INISRGDVVN QEDLYQALAS GQIAAAGLDV TTPEPLPPSH PLLTLKNCVI LPHIGSATYK
     TRNTMSLLAA NNLLAGLRGE AMPSELKL
//
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