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Identification
HMDB Protein ID HMDBP00391
Secondary Accession Numbers
  • 5628
  • HMDBP07391
Name Glyoxylate reductase/hydroxypyruvate reductase
Synonyms
  1. SubName: Glyoxylate reductase/hydroxypyruvate reductase, isoform CRA_b
  2. SubName: cDNA, FLJ96788, Homo sapiens glyoxylate reductase/hydroxypyruvate reductase(GRHPR), mRNA
Gene Name GRHPR
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific Function Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
Pathways
  • Glycine, serine and threonine metabolism
  • Glyoxylate and dicarboxylate metabolism
  • Leigh Syndrome
  • Primary hyperoxaluria II, PH2
  • Pyruvate Decarboxylase E1 Component Deficiency (PDHE1 Deficiency)
  • Pyruvate Dehydrogenase Complex Deficiency
  • Pyruvate kinase deficiency
  • Pyruvate Metabolism
  • Pyruvate metabolism
Reactions
Glycolic acid + NADP → Glyoxylic acid + NADPH details
Glyceric acid + NAD(P)(+) → Hydroxypyruvic acid + NAD(P)H details
Glycolic acid + NADP → Glyoxylic acid + NADPH + Hydrogen Ion details
Glyceric acid + NAD → Hydroxypyruvic acid + NADH + Hydrogen Ion details
Glyceric acid + NADP → Hydroxypyruvic acid + NADPH + Hydrogen Ion details
D-Lactaldehyde + NAD → Pyruvaldehyde + NADH + Hydrogen Ion details
GO Classification
Biological Process
cellular nitrogen compound metabolic process
glyoxylate metabolic process
protein oligomerization
excretion
Cellular Component
peroxisomal matrix
Function
binding
nucleotide binding
catalytic activity
nad or nadh binding
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
cofactor binding
oxidoreductase activity, acting on ch-oh group of donors
oxidoreductase activity
Molecular Function
NAD binding
glycerate dehydrogenase activity
glyoxylate reductase (NADP) activity
hydroxypyruvate reductase activity
protein homodimerization activity
NADPH binding
Process
metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 9
Locus 9q12
SNPs GRHPR
Gene Sequence
>987 bp
ATGAGACCGGTGCGACTCATGAAGGTGTTCGTCACCCGCAGGATACCCGCCGAGGGTAGG
GTCGCGCTCGCCCGGGCGGCAGACTGTGAGGTGGAGCAGTGGGACTCGGATGAGCCCATC
CCTGCCAAGGAGCTAGAGCGAGGTGTGGCGGGGGCCCACGGCCTGCTCTGCCTCCTCTCC
GACCACGTGGACAAGAGGATCCTGGATGCTGCAGGGGCCAATCTCAAAGTCATCAGCACC
ATGTCTGTGGGCATCGACCACTTGGCTTTGGATGAAATCAAGAAGCGTGGGATCCGAGTT
GGCTACACCCCAGATGTCCTGACAGATACCACCGCCGAACTCGCAGTCTCCCTGCTACTT
ACCACCTGCCGCCGGTTGCCGGAGGCCATCGAGGAAGTGAAGAATGGTGGCTGGACCTCG
TGGAAGCCCCTCTGGCTGTGTGGCTATGGACTCACGCAGAGCACTGTCGGCATCATCGGG
CTGGGGCGCATAGGCCAGGCCATTGCTCGGCGTCTGAAACCATTCGGTGTCCAGAGATTT
CTGTACACAGGGCGCCAGCCCAGGCCTGAGGAAGCAGCAGAATTCCAGGCAGAGTTTGTG
TCTACCCCTGAGCTGGCTGCCCAATCTGATTTCATCGTCGTGGCCTGCTCCTTAACACCT
GCAACCGAGGGACTCTGCAACAAGGACTTCTTCCAGAAGATGAAGGAAACAGCTGTGTTC
ATCAACATCAGCAGGGGCGACGTCGTAAACCAGGACGACCTGTACCAGGCCTTGGCCAGT
GGTAAGATTGCAGCTGCTGGACTGGATGTGACGAGCCCAGAACCACTGCCTACAAACCAC
CCTCTCCTGACCCTGAAGAACTGTGTGATTCTGCCCCACATTGGCAGTGCCACCCACAGA
ACCCGCAACACCATGTCCTTGTTGGCAGCTAACAACTTGCTGGCTGGCCTGAGAGGGGAG
CCGATGCCTAGTGAACTCAAGCTGTAG
Protein Properties
Number of Residues 328
Molecular Weight 35667.875
Theoretical pI 7.382
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glyoxylate reductase/hydroxypyruvate reductase
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
GenBank ID Protein 6002730
UniProtKB/Swiss-Prot ID Q9UBQ7
UniProtKB/Swiss-Prot Entry Name GRHPR_HUMAN
PDB IDs
GenBank Gene ID AF134895
GeneCard ID GRHPR
GenAtlas ID GRHPR
HGNC ID HGNC:4570
References
General References
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  2. Rumsby G, Cregeen DP: Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase. Biochim Biophys Acta. 1999 Sep 3;1446(3):383-8. [PubMed:10524214 ]
  3. Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP: The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II. Hum Mol Genet. 1999 Oct;8(11):2063-9. [PubMed:10484776 ]
  4. Huang T, Yang W, Pereira AC, Craigen WJ, Shih VE: Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q. Biochem Biophys Res Commun. 2000 Feb 16;268(2):298-301. [PubMed:10679197 ]
  5. Booth MP, Conners R, Rumsby G, Brady RL: Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase. J Mol Biol. 2006 Jun 30;360(1):178-89. Epub 2006 May 22. [PubMed:16756993 ]
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