GMP reductase 1

NameGMP reductase 1
Synonyms
  • 1.7.1.7
  • GMPR 1
  • GMPR1
  • Guanosine 5'-monophosphate oxidoreductase 1
  • Guanosine monophosphate reductase 1
Gene NameGMPR
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010964|GMP reductase 1
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGT
FEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAV
PQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGV
GPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVM
LGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGD
VENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
Number of residues345
Molecular Weight37418.58
Theoretical pI7.08
GO Classification
Functions
  • metal ion binding
  • GMP reductase activity
Processes
  • small molecule metabolic process
  • nucleobase-containing small molecule metabolic process
  • purine nucleobase metabolic process
  • purine-containing compound salvage
  • response to cold
  • nucleotide metabolic process
Components
  • cytosol
  • GMP reductase complex
General FunctionMetal ion binding
Specific FunctionCatalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID529232
UniProtKB IDP36959
UniProtKB Entry NameGMPR1_HUMAN
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0010965|GMP reductase 1 (GMPR)
ATGCCCCGCATAGATGCGGACCTCAAGCTCGACTTCAAGGATGTCCTGCTCCGACCTAAG
CGGAGCAGCCTCAAGAGCCGAGCCGAGGTGGATCTTGAACGCACCTTCACGTTTCGAAAT
TCAAAGCAGACCTACTCAGGGATTCCCATCATCGTGGCCAACATGGACACTGTGGGCACG
TTTGAGATGGCAGCCGTGATGTCACAGCACTCCATGTTTACAGCAATTCATAAGCATTAC
TCCCTGGATGACTGGAAGCTCTTTGCCACAAATCACCCAGAATGCCTGCAGAATGTAGCC
GTGAGTTCAGGCAGTGGGCAGAATGATCTGGAAAAGATGACCAGCATCCTGGAAGCTGTG
CCACAGGTTAAGTTTATTTGCCTGGATGTGGCCAATGGGTATTCAGAACATTTTGTGGAA
TTCGTGAAACTTGTCCGTGCCAAATTTCCTGAACACACCATTATGGCAGGGAACGTGGTG
ACAGGAGAAATGGTAGAAGAGCTTATTCTTTCCGGAGCAGATATCATCAAAGTGGGAGTT
GGACCAGGTTCTGTGTGCACCACCCGCACCAAGACGGGAGTGGGGTACCCCCAGCTGAGT
GCCGTCATTGAGTGTGCCGACTCTGCCCATGGCCTGAAGGGCCACATCATCTCTGATGGA
GGCTGTACGTGTCCAGGGGATGTCGCCAAAGCCTTTGGAGCTGGAGCAGATTTTGTCATG
CTGGGAGGAATGTTTTCGGGTCATACGGAGTGTGCTGGAGAAGTGTTTGAGAGGAACGGA
CGGAAGCTCAAGCTCTTCTACGGGATGAGCTCTGACACCGCCATGAACAAGCACGCAGGA
GGAGTTGCTGAGTACAGAGCCTCTGAGGGTAAGACTGTGGAAGTTCCTTACAAAGGAGAT
GTGGAAAACACTATCCTGGATATTCTCGGGGGACTGAGGTCCACGTGCACCTACGTGGGG
GCCGCCAAACTCAAGGAGCTCAGCAGGAGGGCAACATTCATCCGGGTGACCCAGCAGCAC
AACACCGTGTTCAGCTAA
GenBank Gene IDL35304
GeneCard IDNot Available
GenAtlas IDGMPR
HGNC IDHGNC:4376
Chromosome Location6
Locus6p23
References
  1. Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. 2758468
  2. Kondoh T, Kanno H, Chang L, Yoshida A: Genomic structure and expression of human guanosine monophosphate reductase. Hum Genet. 1991 Dec;88(2):219-24. 1661705
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  5. Henikoff S, Smith JM: The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase. Cell. 1989 Sep 22;58(6):1021-2. 2570640
  6. Yoshida A, Kan YW: Origin of "fused" glucose-6-phosphate dehydrogenase. Cell. 1990 Jul 13;62(1):11-2. 1694726
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