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Identification
HMDB Protein ID HMDBP00597
Secondary Accession Numbers
  • 5869
  • HMDBP09247
Name AMP deaminase 3
Synonyms
  1. AMP deaminase isoform E
  2. Erythrocyte AMP deaminase
  3. SubName: Adenosine monophosphate deaminase (Isoform E), isoform CRA_b
  4. SubName: cDNA FLJ76195, highly similar to Homo sapiens adenosine monophosphate deaminase (isoform E) (AMPD3),mRNA
Gene Name AMPD3
Protein Type Enzyme
Biological Properties
General Function Involved in deaminase activity
Specific Function AMP deaminase plays a critical role in energy metabolism.
Pathways
  • IMP biosynthesis via salvage pathway
  • Purine metabolism
Reactions
Adenosine monophosphate + Water → Inosinic acid + Ammonia details
GO Classification
Biological Process
purine nucleobase metabolic process
AMP catabolic process
purine-containing compound salvage
IMP salvage
Cellular Component
cytosol
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
amp deaminase activity
deaminase activity
Molecular Function
metal ion binding
AMP deaminase activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
cellular aromatic compound metabolic process
purine nucleoside monophosphate biosynthetic process
purine ribonucleoside monophosphate biosynthetic process
purine base metabolic process
cellular metabolic process
nucleobase metabolic process
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location 11
Locus 11p15
SNPs AMPD3
Gene Sequence
>2304 bp
ATGCCGCGGCAGTTTCCCAAGCTGAACATCTCTGAAGTGGATGAGCAAGTCCGGCTCCTG
GCGGAGAAGGTGTTTGCTAAAGTGCTCCGAGAAGAGGACAGCAAAGATGCCCTGTCCCTG
TTCACTGTCCCAGAGGACTGCCCCATCGGGCAAAAGGAAGCCAAGGAGAGGGAGCTGCAG
AAGGAGCTGGCAGAGCAGAAGTCTGTGGAGACCGCAAAAAGAAAGAAAAGTTTCAAGATG
ATTCGGTCCCAGTCCCTGTCTCTGCAAATGCCGCCACAGCAAGATTGGAAGGGCCCCCCG
GCAGCCAGTCCGGCCATGTCTCCCACAACCCCTGTGGTCACTGGAGCCACTTCCCTGCCC
ACGCCAGCACCCTATGCCATGCCTGAGTTCCAGCGGGTCACCATCAGCGGAGATTACTGT
GCCGGGATCACTTTGGAGGACTATGAGCAGGCAGCCAAGAGTCTGGCCAAGGCCCTAATG
ATCCGGGAGAAGTATGCGCGGCTCGCCTACCACCGCTTCCCGCGGATCACATCCCAGTAC
CTGGGTCATCCGCGGGCGGATACTGCACCTCCGGAAGAGGGCCTTCCAGACTTCCACCCT
CCTCCACTGCCCCAGGAAGACCCCTACTGCCTGGATGATGCACCCCCCAACCTGGATTAC
TTGGTCCACATGCAGGGGGGCATCCTCTTTGTGTATGATAACAAGAAGATGCTGGAGCAC
CAGGAGCCGCACAGCCTACCCTACCCCGACCTGGAGACCTACACGGTGGACATGAGCCAC
ATCCTGGCTCTCATCACCGATGGCCCCACGAAAACCTATTGTCACCGGCGACTGAACTTT
CTGGAATCCAAGTTCAGCCTTCATGAGATGTTAAACGAAATGTCCGAGTTCAAAGAGTTG
AAGAGTAACCCCCACCGGGACTTCTATAACGTGAGAAAGGTGGACACACACATCCATGCG
GCCGCCTGCATGAACCAAAAGCATCTGCTGCGCTTCATCAAGCACACATACCAGACGGAG
CCTGACAGGACTGTGGCAGAGAAGCGGGGCCGGAAGATCACCCTGCGGCAGGTGTTTGAC
GGCCTGCACATGGACCCCTACGACCTCACTGTGGACTCACTGGATGTCCACGCGGGCCGG
CAGACATTCCACCGCTTTGACAAGTTCAACTCCAAATACAACCCTGTGGGGGCCAGTGAG
CTGCGTGACCTGTATTTGAAAACTGAAAACTATCTGGGAGGAGAGTACTTTGCTCGGATG
GTCAAGGAGGTTGCCCGGGAGCTGGAGGAGAGCAAGTACCAGTACTCAGAGCCACGGCTC
TCCATCTACGGCCGCAGTCCTGAGGAGTGGCCCAACCTGGCCTACTGGTTCATCCAGCAC
AAGGTCTACTCTCCCAACATGCGCTGGATCATCCAGGTGCCCCGGATTTATGACATATTT
AGGTCAAAGAAGCTGCTGCCAAACTTTGGGAAGATGCTGGAGAACATCTTCCTGCCCCTT
TTCAAGGCCACTATCAACCCCCAAGATCATCGAGAGCTTCACCTCTTCCTTAAATATGTG
ACGGGGTTTGACAGCGTGGATGATGAGTCCAAGCACAGCGACCACATGTTTTCCGACAAG
AGCCCAAACCCGGACGTCTGGACCAGTGAGCAGAACCCACCCTACAGCTACTACCTGTAC
TACATGTATGCCAACATCATGGTGCTCAACAACCTCCGCAGGGAGCGCGGCCTGAGCACG
TTCCTGTTCCGGCCGCACTGTGGGGAAGCCGGCTCCATCACCCACCTGGTGTCTGCCTTC
CTCACTGCTGACAACATTTCCCACGGGCTGCTCCTCAAGAAGAGTCCGGTATTGCAGTAT
CTCTACTACCTTGCTCAGATCCCCATTGCCATGTCTCCTCTTAGCAACAACAGTTTGTTC
CTCGAATATTCCAAGAACCCTCTGAGGGAATTCCTACACAAGGGACTGCATGTTTCTCTT
TCCACCGATGACCCCATGCAGTTCCACTACACGAAGGAAGCACTTATGGAAGAATATGCC
ATTGCAGCTCAAGTGTGGAAGCTGAGCACCTGCGACCTGTGTGAGATCGCCAGGAACAGC
GTGCTGCAGAGCGGCCTCTCGCATCAGGAAAAGCAAAAGTTTCTGGGACAAAATTATTAT
AAAGAAGGACCTGAAGGAAATGATATTCGAAAGACAAATGTGGCTCAGATCCGGATGGCA
TTCCGATATGAGACCTTATGCAATGAGCTCAGCTTCCTGTCTGATGCTATGAAATCAGAA
GAGATCACCGCCTTGACCAACTAG
Protein Properties
Number of Residues 767
Molecular Weight 89727.485
Theoretical pI 6.849
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>AMP deaminase 3
MPRQFPKLNISEVDEQVRLLAEKVFAKVLREEDSKDALSLFTVPEDCPIGQKEAKERELQ
KELAEQKSVETAKRKKSFKMIRSQSLSLQMPPQQDWKGPPAASPAMSPTTPVVTGATSLP
TPAPYAMPEFQRVTISGDYCAGITLEDYEQAAKSLAKALMIREKYARLAYHRFPRITSQY
LGHPRADTAPPEEGLPDFHPPPLPQEDPYCLDDAPPNLDYLVHMQGGILFVYDNKKMLEH
QEPHSLPYPDLETYTVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKEL
KSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKRGRKITLRQVFD
GLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARM
VKEVARELEESKYQYSEPRLSIYGRSPEEWPNLAYWFIQHKVYSPNMRWIIQVPRIYDIF
RSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDK
SPNPDVWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAF
LTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSL
STDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYY
KEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTN
GenBank ID Protein 158261019
UniProtKB/Swiss-Prot ID Q01432
UniProtKB/Swiss-Prot Entry Name AMPD3_HUMAN
PDB IDs Not Available
GenBank Gene ID D12775
GeneCard ID AMPD3
GenAtlas ID AMPD3
HGNC ID HGNC:470
References
General References
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  4. Yamada Y, Goto H, Ogasawara N: Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase. Biochim Biophys Acta. 1992 Nov 15;1171(1):125-8. [PubMed:1420359 ]
  5. Mahnke-Zizelman DK, Sabina RL: Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. J Biol Chem. 1992 Oct 15;267(29):20866-77. [PubMed:1400401 ]
  6. Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL: Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing. Biochim Biophys Acta. 1996 Apr 10;1306(1):75-92. [PubMed:8611627 ]
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  8. Yamada Y, Goto H, Murase T, Ogasawara N: Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations. Hum Mol Genet. 1994 Dec;3(12):2243-5. [PubMed:7881427 ]
  9. Yamada Y, Makarewicz W, Goto H, Nomura N, Kitoh H, Ogasawara N: Gene mutations responsible for human erythrocyte AMP deaminase deficiency in Poles. Adv Exp Med Biol. 1998;431:347-50. [PubMed:9598089 ]
  10. Yamada Y, Goto H, Wakamatsu N, Ogasawara N: A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3. Hum Mutat. 2001;17(1):78. [PubMed:11139257 ]
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