Adenylosuccinate synthetase
Details
- Name
- Adenylosuccinate synthetase
- Synonyms
- 6.3.4.4
- AMPSase
- IMP--aspartate ligase
- Gene Name
- Adss
- Organism
- Plasmodium falciparum
- Amino acid sequence
>lcl|BSEQ0019317|Adenylosuccinate synthetase MNIFDHQIKNVDKGNVVAILGAQWGDEGKGKIIDMLSEYSDITCRFNGGANAGHTISVND KKYALHLLPCGVLYDNNISVLGNGMVIHVKSLMEEIESVGGKLLDRLYLSNKAHILFDIH QIIDSIQETKKLKEGKQIGTTKRGIGPCYSTKASRIGIRLGTLKNFENFKNMYSKLIDHL MDLYNITEYDKEKELNLFYNYHIKLRDRIVDVISFMNTNLENNKKVLIEGANAAMLDIDF GTYPYVTSSCTTVGGVFSGLGIHHKKLNLVVGVVKSYLTRVGCGPFLTELNNDVGQYLRE KGHEYGTTTKRPRRCGWLDIPMLLYVKCINSIDMINLTKLDVLSGLEEILLCVNFKNKKT GELLEKGCYPVEEEISEEYEPVYEKFSGWKEDISTCNEFDELPENAKKYILAIEKYLKTP IVWIGVGPNRKNMIVKKNFNLN
- Number of residues
- 442
- Molecular Weight
- 50064.525
- Theoretical pI
- 7.71
- GO Classification
- Functionsadenylosuccinate synthase activity / GTP binding / metal ion bindingProcesses'de novo' AMP biosynthetic processComponentscytoplasm
- General Function
- Metal ion binding
- Specific Function
- Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
- Pfam Domain Function
- Adenylsucc_synt (PF00709)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0005295|1323 bp ATATTTGATCATCAAATAAAAAATGTGGATAAAGGGAATGTAGTTGCAATATTAGGTGCA CAATGGGGTGATGAAGGGAAAGGAAAAATAATTGATATGTTATCAGAATATTCTGATATT ACTTGTAGATTTAATGGAGGTGCTAATGCAGGACATACGATATCAGTAAATGATAAGAAA TATGCTTTACATTTATTACCATGTGGTGTATTATATGATAATAATATAAGTGTATTAGGA AACGGAATGGTAATACATGTAAAATCATTAATGGAAGAAATTGAATCAGTTGGGGGAAAG TTGTTAGATAGATTATATTTATCAAATAAAGCACATATATTATTTGATATTCATCAAATT ATTGATTCAATCCAAGAAACGAAAAAATTGAAAGAAGGAAAACAAATAGGTACAACAAAA AGAGGTATTGGACCATGTTATTCTACTAAAGCTTCCAGAATAGGTATAAGATTAGGAACT TTAAAAAATTTTGAAAATTTTAAAAATATGTATAGTAAATTAATAGACCACTTAATGGAT TTATATAATATAACAGAATATGACAAAGAAAAAGAACTCAACTTATTTTATAATTATCAC ATAAAGTTAAGAGATAGAATAGTTGATGTTATTTCCTTTATGAATACAAATTTAGAAAAC AACAAAAAAGTATTAATTGAAGGTGCTAATGCAGCTATGTTAGATATTGATTTTGGAACA TATCCATATGTAACTAGTAGCTGTACAACAGTTGGTGGGGTTTTCTCAGGACTTGGAATT CATCATAAAAAACTGAATTTAGTTGTAGGTGTAGTTAAAAGTTACTTAACCAGAGTTGGA TGTGGCCCTTTCTTAACTGAATTAAATAATGACGTTGGTCAATATTTAAGAGAAAAAGGT CATGAATATGGAACGACTACCAAGAGACCAAGAAGGTGTGGATGGCTCGACATACCAATG TTATTATATGTTAAGTGCATTAATAGTATTGATATGATAAACTTAACAAAATTGGATGTT TTATCTGGATTAGAGGAAATATTATTGTGTGTCAATTTTAAAAATAAAAAAACAGGAGAA CTGCTTGAAAAGGGTTGCTACCCTGTTGAAGAAGAAATATCAGAAGAATATGAACCTGTT TATGAAAAATTCAGTGGATGGAAAGAAGACATCTCAACTTGTAATGAATTTGATGAATTA CCAGAAAATGCAAAAAAATATATTTTAGCTATAGAGAAATATTTAAAAACTCCAATAGTT TGGATTGGTGTAGGTCCTAATAGAAAAAATATGATAGTTAAAAAGAATTTTAACCTAAAC TAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9U8D3 UniProtKB Entry Name PURA_PLAFA GenBank Gene ID AF095282 - General References
- Jayalakshmi R, Sumathy K, Balaram H: Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli. Protein Expr Purif. 2002 Jun;25(1):65-72. [Article]
- Raman J, Mehrotra S, Anand RP, Balaram H: Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase. Mol Biochem Parasitol. 2004 Nov;138(1):1-8. [Article]
- Mehrotra S, Mylarappa BN, Iyengar P, Balaram H: Studies on active site mutants of P. falciparum adenylosuccinate synthetase: insights into enzyme catalysis and activation. Biochim Biophys Acta. 2010 Oct;1804(10):1996-2002. doi: 10.1016/j.bbapap.2010.07.015. Epub 2010 Aug 1. [Article]
- Eaazhisai K, Jayalakshmi R, Gayathri P, Anand RP, Sumathy K, Balaram H, Murthy MR: Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum. J Mol Biol. 2004 Jan 30;335(5):1251-64. [Article]