GRHPR_HUMAN
ID GRHPR_HUMAN Reviewed; 328 AA.
AC Q9UBQ7; Q5T945; Q9H3E9; Q9H636; Q9UKX1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase;
DE EC=1.1.1.79 {ECO:0000269|PubMed:10484776, ECO:0000269|PubMed:10524214};
DE EC=1.1.1.81 {ECO:0000269|PubMed:10484776, ECO:0000269|PubMed:10524214};
GN Name=GRHPR; Synonyms=GLXR; ORFNames=MSTP035;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=10524214; DOI=10.1016/s0167-4781(99)00105-0;
RA Rumsby G., Cregeen D.P.;
RT "Identification and expression of a cDNA for human
RT hydroxypyruvate/glyoxylate reductase.";
RL Biochim. Biophys. Acta 1446:383-388(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INVOLVEMENT IN HP2,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=10484776; DOI=10.1093/hmg/8.11.2063;
RA Cramer S.D., Ferree P.M., Lin K., Milliner D.S., Holmes R.P.;
RT "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients
RT with primary hyperoxaluria type II.";
RL Hum. Mol. Genet. 8:2063-2069(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-328 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10679197; DOI=10.1006/bbrc.2000.2122;
RA Huang T., Yang W., Pereira A.C., Craigen W.J., Shih V.E.;
RT "Cloning and characterization of a putative human D-2-hydroxyacid
RT dehydrogenase in chromosome 9q.";
RL Biochem. Biophys. Res. Commun. 268:298-301(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-272 AND THR-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE,
RP AND SUBUNIT.
RX PubMed=16756993; DOI=10.1016/j.jmb.2006.05.018;
RA Booth M.P.S., Conners R., Rumsby G., Brady R.L.;
RT "Structural basis of substrate specificity in human glyoxylate
RT reductase/hydroxypyruvate reductase.";
RL J. Mol. Biol. 360:178-189(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-328.
RG Center for eukaryotic structural genomics (CESG);
RT "Crystal structure of a glyoxylate/hydroxypyruvate reductase from Homo
RT sapiens.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase
CC and D-glycerate dehydrogenase enzymatic activities. Reduces
CC hydroxypyruvate to D-glycerate, glyoxylate to glycolate, oxidizes D-
CC glycerate to hydroxypyruvate. {ECO:0000269|PubMed:10484776,
CC ECO:0000269|PubMed:10524214}.
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; EC=1.1.1.79;
CC Evidence={ECO:0000269|PubMed:10484776, ECO:0000269|PubMed:10524214};
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=1.1.1.81;
CC Evidence={ECO:0000269|PubMed:10484776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC Evidence={ECO:0000269|PubMed:10484776, ECO:0000269|PubMed:10524214};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10524214,
CC ECO:0000269|PubMed:16756993}.
CC -!- INTERACTION:
CC Q9UBQ7; Q9UHI7: SLC23A1; NbExp=6; IntAct=EBI-372445, EBI-1759386;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBQ7-2; Sequence=VSP_057016, VSP_057017, VSP_057018;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundantly expressed in the liver.
CC {ECO:0000269|PubMed:10679197}.
CC -!- DISEASE: Hyperoxaluria primary 2 (HP2) [MIM:260000]: A disorder
CC characterized by elevated urinary excretion of oxalate and L-glycerate,
CC progressive tissue accumulation of insoluble calcium oxalate,
CC nephrolithiasis, nephrocalcinosis, and end-stage renal disease.
CC {ECO:0000269|PubMed:10484776}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD54066.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG39286.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF134895; AAF00111.1; -; mRNA.
DR EMBL; AF146018; AAD45886.1; -; mRNA.
DR EMBL; AF146689; AAD46517.1; -; Genomic_DNA.
DR EMBL; AF113215; AAG39286.1; ALT_FRAME; mRNA.
DR EMBL; AK026287; BAB15430.1; -; mRNA.
DR EMBL; AK315690; BAG38053.1; -; mRNA.
DR EMBL; AL158155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58284.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58285.1; -; Genomic_DNA.
DR EMBL; BC000605; AAH00605.1; -; mRNA.
DR EMBL; AF113251; AAD54066.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6609.1; -. [Q9UBQ7-1]
DR PIR; JC7190; JC7190.
DR RefSeq; NP_036335.1; NM_012203.1. [Q9UBQ7-1]
DR PDB; 2GCG; X-ray; 2.20 A; A/B/C/D=1-328.
DR PDB; 2H1S; X-ray; 2.45 A; A/B/C/D=2-328.
DR PDB; 2Q50; X-ray; 2.45 A; A/B/C/D=2-328.
DR PDB; 2WWR; X-ray; 2.82 A; A/B/C/D=1-328.
DR PDBsum; 2GCG; -.
DR PDBsum; 2H1S; -.
DR PDBsum; 2Q50; -.
DR PDBsum; 2WWR; -.
DR AlphaFoldDB; Q9UBQ7; -.
DR SMR; Q9UBQ7; -.
DR BioGRID; 114781; 91.
DR IntAct; Q9UBQ7; 17.
DR MINT; Q9UBQ7; -.
DR STRING; 9606.ENSP00000313432; -.
DR ChEMBL; CHEMBL4295972; -.
DR iPTMnet; Q9UBQ7; -.
DR MetOSite; Q9UBQ7; -.
DR PhosphoSitePlus; Q9UBQ7; -.
DR SwissPalm; Q9UBQ7; -.
DR BioMuta; GRHPR; -.
DR DMDM; 47116943; -.
DR REPRODUCTION-2DPAGE; IPI00037448; -.
DR UCD-2DPAGE; Q9UBQ7; -.
DR EPD; Q9UBQ7; -.
DR jPOST; Q9UBQ7; -.
DR MassIVE; Q9UBQ7; -.
DR MaxQB; Q9UBQ7; -.
DR PaxDb; Q9UBQ7; -.
DR PeptideAtlas; Q9UBQ7; -.
DR PRIDE; Q9UBQ7; -.
DR ProteomicsDB; 80956; -.
DR ProteomicsDB; 84034; -. [Q9UBQ7-1]
DR Antibodypedia; 11982; 319 antibodies from 27 providers.
DR DNASU; 9380; -.
DR Ensembl; ENST00000318158.11; ENSP00000313432.6; ENSG00000137106.18. [Q9UBQ7-1]
DR Ensembl; ENST00000494290.1; ENSP00000432021.1; ENSG00000137106.18. [Q9UBQ7-2]
DR GeneID; 9380; -.
DR KEGG; hsa:9380; -.
DR MANE-Select; ENST00000318158.11; ENSP00000313432.6; NM_012203.2; NP_036335.1.
DR UCSC; uc003zzu.2; human. [Q9UBQ7-1]
DR CTD; 9380; -.
DR DisGeNET; 9380; -.
DR GeneCards; GRHPR; -.
DR GeneReviews; GRHPR; -.
DR HGNC; HGNC:4570; GRHPR.
DR HPA; ENSG00000137106; Tissue enhanced (liver).
DR MalaCards; GRHPR; -.
DR MIM; 260000; phenotype.
DR MIM; 604296; gene.
DR neXtProt; NX_Q9UBQ7; -.
DR OpenTargets; ENSG00000137106; -.
DR Orphanet; 93599; Primary hyperoxaluria type 2.
DR PharmGKB; PA28965; -.
DR VEuPathDB; HostDB:ENSG00000137106; -.
DR eggNOG; KOG0069; Eukaryota.
DR GeneTree; ENSGT00940000158578; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; Q9UBQ7; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 1378766at2759; -.
DR PhylomeDB; Q9UBQ7; -.
DR TreeFam; TF324791; -.
DR BioCyc; MetaCyc:HS06275-MON; -.
DR BRENDA; 1.1.1.26; 2681.
DR BRENDA; 1.1.1.79; 2681.
DR BRENDA; 1.1.1.81; 2681.
DR PathwayCommons; Q9UBQ7; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR SABIO-RK; Q9UBQ7; -.
DR SignaLink; Q9UBQ7; -.
DR BioGRID-ORCS; 9380; 18 hits in 1078 CRISPR screens.
DR ChiTaRS; GRHPR; human.
DR EvolutionaryTrace; Q9UBQ7; -.
DR GeneWiki; GRHPR; -.
DR GenomeRNAi; 9380; -.
DR Pharos; Q9UBQ7; Tbio.
DR PRO; PR:Q9UBQ7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UBQ7; protein.
DR Bgee; ENSG00000137106; Expressed in right lobe of liver and 210 other tissues.
DR ExpressionAtlas; Q9UBQ7; baseline and differential.
DR Genevisible; Q9UBQ7; HS.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0031406; F:carboxylic acid binding; IEA:Ensembl.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019752; P:carboxylic acid metabolic process; TAS:Reactome.
DR GO; GO:0043648; P:dicarboxylic acid metabolic process; IEA:Ensembl.
DR GO; GO:0046487; P:glyoxylate metabolic process; IDA:UniProtKB.
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 3D-structure; Alternative splicing; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..328
FT /note="Glyoxylate reductase/hydroxypyruvate reductase"
FT /id="PRO_0000075944"
FT ACT_SITE 293
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16756993"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 162..164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 185..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 293..296
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16756993"
FT BINDING 295
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16756993"
FT SITE 274
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000305|PubMed:16756993"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..21
FT /note="MRPVRLMKVFVTRRIPAEGRV -> MLGGVPTLCGTGNETWTLLAL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057016"
FT VAR_SEQ 22..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057017"
FT VAR_SEQ 246..328
FT /note="GDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSA
FT THRTRNTMSLLAANNLLAGLRGEPMPSELKL -> YPRATLPSKPGEEPSPLLPSGDFL
FT PRGLLVRPQAELAGFHKPNNQLRNSWEYTRPPYREEEPSEWAWPVCFSAVAPTRRGLAH
FT SSVASGSVPREPLQAHYPPPQRAGLEDLKGPLEAASHTAEPGFVWLWFSDTLNLMLLGG
FT QTLKLTWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057018"
FT VARIANT 170
FT /note="R -> Q (in dbSNP:rs12002324)"
FT /id="VAR_032762"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2Q50"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:2GCG"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2Q50"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2GCG"
FT TURN 220..224
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:2GCG"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2GCG"
FT HELIX 299..318
FT /evidence="ECO:0007829|PDB:2GCG"
SQ SEQUENCE 328 AA; 35668 MW; 68A0E311AA4E5650 CRC64;
MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS
DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL
TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF
LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF
INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR
TRNTMSLLAA NNLLAGLRGE PMPSELKL
