Hmdb loader
Identification
HMDB Protein ID HMDBP00880
Secondary Accession Numbers
  • 6162
  • HMDBP03773
Name Adenylosuccinate synthetase isozyme 2
Synonyms
  1. AMPSase 2
  2. AdSS 2
  3. Adenylosuccinate synthetase, acidic isozyme
  4. Adenylosuccinate synthetase, liver isozyme
  5. IMP--aspartate ligase 2
  6. L-type adenylosuccinate synthetase
Gene Name ADSS
Protein Type Unknown
Biological Properties
General Function Involved in adenylosuccinate synthase activity
Specific Function Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Pathways
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Alanine, aspartate and glutamate metabolism
  • AMP biosynthesis via de novo pathway
  • Azathioprine Action Pathway
  • Gout or Kelley-Seegmiller Syndrome
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Purine metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Thioguanine Action Pathway
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
Guanosine triphosphate + Inosinic acid + L-Aspartic acid → Guanosine diphosphate + Phosphate + Adenylsuccinic acid details
Guanosine triphosphate + Inosinic acid + L-Aspartic acid → Guanosine diphosphate + Phosphate + Adenylsuccinic acid details
GO Classification
Biological Process
purine nucleobase metabolic process
AMP biosynthetic process
'de novo' AMP biosynthetic process
immune system process
Cellular Component
cytosol
plasma membrane
Component
cell part
intracellular part
cytoplasm
Function
ion binding
cation binding
metal ion binding
purine nucleotide binding
binding
nucleotide binding
catalytic activity
guanyl nucleotide binding
guanyl ribonucleotide binding
gtp binding
adenylosuccinate synthase activity
magnesium ion binding
ligase activity
ligase activity, forming carbon-nitrogen bonds
Molecular Function
magnesium ion binding
GTP binding
adenylosuccinate synthase activity
phosphate ion binding
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 Location
  1. Cytoplasm
Gene Properties
Chromosome Location 1
Locus 1q44
SNPs ADSS
Gene Sequence
>1371 bp
ATGGCGTTCGCCGAGACCTACCCGGCGGCATCCTCCCTGCCCAACGGCGATTGCGGCCGC
CCCAGGGCGCGGCCCGGAGGAAACCGGGTGACGGTGGTGCTCGGTGCGCAGTGGGGCGAC
GAAGGCAAAGGGAAGGTGGTGGACCTGCTGGCGCAGGACGCCGACATCGTGTGCCGCTGC
CAGGGAGGAAATAATGCTGGCCATACAGTTGTTGTGGATTCTGTGGAATATGATTTTCAT
CTCTTACCCAGTGGAATAATTAATCCAAATGTCACTGCATTCATTGGAAATGGTGTGGTA
ATTCATCTACCTGGATTGTTTGAAGAAGCAGAGAAAAATGTTCAAAAAGGAAAAGGACTA
GAAGGCTGGGAAAAAAGGCTTATTATATCTGACAGAGCTCATATTGTATTTGATTTTCAT
CAAGCAGCTGATGGTATCCAGGAACAACAGAGACAAGAACAAGCAGGAAAAAATTTGGGT
ACAACAAAAAAGGGCATTGGCCCAGTTTATTCGTCCAAAGCTGCTCGGAGTGGACTCAGG
ATGTGCGACCTTGTTTCTGACTTTGATGGCTTCTCTGAGAGGTTTAAAGTTCTAGCTAAC
CAATACAAATCTATATACCCCACTTTGGAAATAGACATTGAAGGTGAATTACAAAAACTC
AAGGGTTATATGGAAAAGATTAAACCAATGGTGAGAGATGGAGTTTATTTTCTATATGAG
GCCCTACATGGACCACCAAAGAAAATCTTGGTAGAAGGTGCAAATGCAGCACTATTAGAT
ATTGATTTTGGGACTTACCCTTTTGTAACCTCTTCAAATTGTACTGTTGGAGGTGTTTGT
ACTGGTTTGGGTATGCCACCTCAAAATGTTGGAGAAGTGTATGGAGTTGTGAAAGCTTAT
ACAACTAGAGTTGGTATTGGTGCCTTTCCTACAGAGCAAGACAATGAAATTGGAGAATTA
TTACAAACAAGGGGTAGAGAGTTTGGTGTAACTACTGGAAGGAAAAGAAGATGTGGCTGG
TTGGACCTCGTTTTGCTCAAATATGCTCATATGATCAATGGATTTACTGCGTTGGCACTT
ACCAAGTTGGATATTTTGGACATGTTTACGGAAATCAAAGTTGGAGTTGCTTACAAGTTA
GATGGTGAAATCATACCTCATATCCCAGCAAACCAAGAAGTCTTAAATAAAGTTGAAGTT
CAATATAAGACTCTCCCAGGATGGAACACAGACATATCAAATGCAAGGGCGTTTAAAGAA
CTACCTGTTAATGCACAAAACTATGTTCGATTTATTGAAGATGAGCTTCAAATTCCAGTT
AAGTGGATTGGTGTTGGTAAATCCAGAGAATCTATGATTCAACTCTTTTAA
Protein Properties
Number of Residues 456
Molecular Weight 50097.075
Theoretical pI 6.554
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Adenylosuccinate synthetase isozyme 2
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRC
QGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGL
EGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLR
MCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYE
ALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAY
TTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALAL
TKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKE
LPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
GenBank ID Protein 34577063
UniProtKB/Swiss-Prot ID P30520
UniProtKB/Swiss-Prot Entry Name PURA2_HUMAN
PDB IDs
GenBank Gene ID NM_001126
GeneCard ID ADSS
GenAtlas ID ADSS
HGNC ID HGNC:292
References
General References
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  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Powell SM, Zalkin H, Dixon JE: Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett. 1992 May 25;303(1):4-10. [PubMed:1592113 ]