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NameGuanine deaminase
Synonyms
  • 3.5.4.3
  • GAH
  • Guanase
  • Guanine aminohydrolase
  • KIAA1258
  • p51-nedasin
Gene NameGDA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0009314|Guanine deaminase
MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCF
KPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFA
EEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEY
KETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSH
ISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAH
CPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNE
KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDI
SEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
Number of residues454
Molecular Weight51002.565
Theoretical pINot Available
GO Classification
Functions
  • guanine deaminase activity
  • zinc ion binding
Processes
  • nervous system development
  • nucleobase-containing small molecule metabolic process
  • purine nucleobase metabolic process
  • nucleobase-containing compound metabolic process
  • purine nucleotide catabolic process
  • guanine catabolic process
  • guanine metabolic process
  • small molecule metabolic process
Components
  • intracellular
  • cytosol
  • extracellular exosome
General FunctionZinc ion binding
Specific FunctionCatalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDQ9Y2T3
UniProtKB Entry NameGUAD_HUMAN
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0021457|Guanine deaminase (GDA)
ATGTGTGCCGCTCAGATGCCGCCCCTGGCGCACATCTTCCGAGGGACGTTCGTCCACTCC
ACCTGGACCTGCCCCATGGAGGTGCTGCGGGATCACCTCCTCGGCGTGAGCGACAGCGGC
AAAATAGTGTTTTTAGAAGAAGCATCTCAACAGGAAAAACTGGCCAAAGAATGGTGCTTC
AAGCCGTGTGAAATAAGAGAACTGAGCCACCATGAGTTCTTCATGCCTGGGCTGGTTGAT
ACACACATCCATGCCTCTCAGTATTCCTTTGCTGGAAGTAGCATAGACCTGCCACTCTTG
GAGTGGCTGACCAAGTACACATTTCCTGCAGAACACAGATTCCAGAACATCGACTTTGCA
GAAGAAGTATATACCAGAGTTGTCAGGAGAACACTAAAGAATGGAACAACCACAGCTTGT
TACTTTGCAACAATTCACACTGACTCATCTCTGCTCCTTGCCGACATTACAGATAAATTT
GGACAGCGGGCATTTGTGGGCAAAGTTTGCATGGATTTGAATGACACTTTTCCAGAATAC
AAGGAGACCACTGAGGAATCGATCAAGGAAACTGAGAGATTTGTGTCAGAAATGCTCCAA
AAGAACTATTCTAGAGTGAAGCCCATAGTGACACCACGTTTTTCCCTCTCCTGCTCTGAG
ACTTTGATGGGTGAACTGGGCAACATTGCTAAAACCCGTGATTTGCACATTCAGAGCCAT
ATAAGTGAAAATCGTGATGAAGTTGAAGCTGTGAAAAACTTATACCCCAGTTATAAAAAC
TACACATCTGTGTATGATAAAAACAATCTTTTGACAAATAAGACAGTGATGGCACACGGC
TGCTACCTCTCTGCAGAAGAACTGAACGTATTCCATGAACGAGGAGCATCCATCGCACAC
TGTCCCAATTCTAATTTATCGCTCAGCAGTGGATTTCTAAATGTGCTAGAAGTCCTGAAA
CATGAAGTCAAGATAGGGCTGGGTACAGACGTGGCTGGTGGCTATTCATATTCCATGCTT
GATGCAATCAGAAGAGCAGTGATGGTTTCCAATATCCTTTTAATTAATAAGGTAAATGAG
AAAAGCCTCACCCTCAAAGAAGTCTTCAGACTAGCTACTCTTGGAGGAAGCCAAGCCCTG
GGGCTGGATGGTGAGATTGGAAACTTTGAAGTGGGCAAGGAATTTGATGCCATCCTGATC
AACCCCAAAGCATCCGACTCTCCCATTGACCTGTTTTATGGGGACTTTTTTGGTGATATT
TCTGAGGCTGTTATCCAGAAGTTCCTCTATCTAGGAGATGATCGAAATATTGAAGAGGTT
TATGTGGGCGGAAAGCAGGTGGTTCCGTTTTCCAGCTCAGTGAAAGAAACAATTCACTTA
CCAGCCTCCTCACCCCATCCTCCACCATTTCCTTAA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:4212
Chromosome Location9
LocusNot Available
References
  1. Yuan G, Bin JC, McKay DJ, Snyder FF: Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein. J Biol Chem. 1999 Mar 19;274(12):8175-80. 10075721
  2. Kuwahara H, Araki N, Makino K, Masuko N, Honda S, Kaibuchi K, Fukunaga K, Miyamoto E, Ogawa M, Saya H: A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor. J Biol Chem. 1999 Nov 5;274(45):32204-14. 10542258
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