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Protein

Adenylosuccinate synthetase

Gene

Adss

Organism
Plasmodium falciparum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity3 Publications

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Enzyme regulationi

Inhibited by hadacidin. Activated by fructose 1,6-bisphosphate.2 Publications

Kineticsi

  1. KM=18.4 µM for GTP2 Publications
  2. KM=23 µM for IMP2 Publications
  3. KM=1800 µM for L-aspartate2 Publications

    pH dependencei

    Optimum pH is 6.8-7.5.2 Publications

    Pathwayi: AMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Adenylosuccinate synthetase (Adss)
    2. Adenylosuccinate lyase (adsl), Adenylosuccinate lyase (adsl), Adenylosuccinate lyase (adsl), Adenylosuccinate lyase (adsl), Adenylosuccinate lyase (adsl), Adenylosuccinate lyase (adsl)
    This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei26 – 261Proton acceptorUniRule annotation
    Metal bindingi26 – 261MagnesiumUniRule annotation
    Metal bindingi53 – 531Magnesium; via carbonyl oxygenUniRule annotation
    Active sitei54 – 541Proton donorUniRule annotation
    Binding sitei62 – 621GTPUniRule annotation
    Binding sitei141 – 1411IMPUniRule annotation
    Binding sitei155 – 1551IMP; shared with dimeric partnerUniRule annotation
    Binding sitei232 – 2321IMPUniRule annotation
    Binding sitei247 – 2471IMPUniRule annotation
    Binding sitei307 – 3071GTPUniRule annotation
    Binding sitei311 – 3111IMPUniRule annotation
    Binding sitei313 – 3131GTPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi25 – 317GTPUniRule annotation
    Nucleotide bindingi53 – 553GTPUniRule annotation
    Nucleotide bindingi339 – 3413GTPUniRule annotation
    Nucleotide bindingi425 – 4273GTPUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.4.4. 4889.
    UniPathwayiUPA00075; UER00335.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate synthetaseUniRule annotation (EC:6.3.4.4UniRule annotation)
    Short name:
    AMPSaseUniRule annotation
    Short name:
    AdSSUniRule annotation
    Alternative name(s):
    IMP--aspartate ligaseUniRule annotation
    Gene namesi
    Name:Adss
    OrganismiPlasmodium falciparum
    Taxonomic identifieri5833 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 442442Adenylosuccinate synthetasePRO_0000399294Add
    BLAST

    Proteomic databases

    PaxDbiQ9U8D3.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi5833.PF13_0287.

    Structurei

    Secondary structure

    1
    442
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 2510Combined sources
    Helixi29 – 368Combined sources
    Helixi37 – 393Combined sources
    Beta strandi41 – 455Combined sources
    Beta strandi54 – 585Combined sources
    Beta strandi61 – 688Combined sources
    Turni70 – 734Combined sources
    Beta strandi78 – 814Combined sources
    Helixi89 – 9911Combined sources
    Helixi103 – 1064Combined sources
    Beta strandi107 – 1104Combined sources
    Beta strandi113 – 1153Combined sources
    Helixi118 – 13316Combined sources
    Beta strandi142 – 1443Combined sources
    Helixi145 – 1539Combined sources
    Helixi160 – 1645Combined sources
    Helixi166 – 18318Combined sources
    Helixi191 – 20515Combined sources
    Helixi206 – 2083Combined sources
    Helixi212 – 22110Combined sources
    Beta strandi226 – 2294Combined sources
    Helixi234 – 2363Combined sources
    Turni238 – 2403Combined sources
    Helixi253 – 2586Combined sources
    Turni259 – 2613Combined sources
    Helixi264 – 2663Combined sources
    Beta strandi269 – 28012Combined sources
    Beta strandi282 – 2843Combined sources
    Helixi293 – 3019Combined sources
    Turni307 – 3093Combined sources
    Beta strandi314 – 3163Combined sources
    Helixi320 – 33011Combined sources
    Beta strandi333 – 3386Combined sources
    Helixi340 – 3434Combined sources
    Beta strandi347 – 35711Combined sources
    Turni358 – 3603Combined sources
    Helixi373 – 3764Combined sources
    Beta strandi379 – 3879Combined sources
    Helixi399 – 4013Combined sources
    Helixi404 – 41714Combined sources
    Beta strandi421 – 4255Combined sources
    Beta strandi427 – 4293Combined sources
    Beta strandi433 – 4353Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P9BX-ray2.00A3-442[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9U8D3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 294IMP bindingUniRule annotation
    Regioni51 – 544IMP bindingUniRule annotation
    Regioni307 – 3137Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiKOG1355. Eukaryota.
    COG0104. LUCA.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
    IPR033128. Adenylosuccin_syn_Lys_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11846. PTHR11846. 1 hit.
    PfamiPF00709. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SMARTiSM00788. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00184. purA. 1 hit.
    PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9U8D3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNIFDHQIKN VDKGNVVAIL GAQWGDEGKG KIIDMLSEYS DITCRFNGGA
    60 70 80 90 100
    NAGHTISVND KKYALHLLPC GVLYDNNISV LGNGMVIHVK SLMEEIESVG
    110 120 130 140 150
    GKLLDRLYLS NKAHILFDIH QIIDSIQETK KLKEGKQIGT TKRGIGPCYS
    160 170 180 190 200
    TKASRIGIRL GTLKNFENFK NMYSKLIDHL MDLYNITEYD KEKELNLFYN
    210 220 230 240 250
    YHIKLRDRIV DVISFMNTNL ENNKKVLIEG ANAAMLDIDF GTYPYVTSSC
    260 270 280 290 300
    TTVGGVFSGL GIHHKKLNLV VGVVKSYLTR VGCGPFLTEL NNDVGQYLRE
    310 320 330 340 350
    KGHEYGTTTK RPRRCGWLDI PMLLYVKCIN SIDMINLTKL DVLSGLEEIL
    360 370 380 390 400
    LCVNFKNKKT GELLEKGCYP VEEEISEEYE PVYEKFSGWK EDISTCNEFD
    410 420 430 440
    ELPENAKKYI LAIEKYLKTP IVWIGVGPNR KNMIVKKNFN LN
    Length:442
    Mass (Da):50,065
    Last modified:October 5, 2010 - v3
    Checksum:iE20F5E1D36B34C4E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF095282 mRNA. Translation: AAF06822.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF095282 mRNA. Translation: AAF06822.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P9BX-ray2.00A3-442[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5833.PF13_0287.

    Proteomic databases

    PaxDbiQ9U8D3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiKOG1355. Eukaryota.
    COG0104. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00075; UER00335.
    BRENDAi6.3.4.4. 4889.

    Miscellaneous databases

    EvolutionaryTraceiQ9U8D3.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
    IPR033128. Adenylosuccin_syn_Lys_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11846. PTHR11846. 1 hit.
    PfamiPF00709. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SMARTiSM00788. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00184. purA. 1 hit.
    PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli."
      Jayalakshmi R., Sumathy K., Balaram H.
      Protein Expr. Purif. 25:65-72(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: T9/106.
    2. "Cloning and characterization of the Plasmodium falciparum adenylosuccinate synthetase gene."
      Sumathy K., Jayalakshmi R., Shivayogi M.S., Balaram H.
      Curr. Sci. 78:101-105(2000)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-442, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
      Strain: T9/106.
    3. "Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase."
      Raman J., Mehrotra S., Anand R.P., Balaram H.
      Mol. Biochem. Parasitol. 138:1-8(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: T9/106.
    4. "Studies on active site mutants of P. falciparum adenylosuccinate synthetase: Insights into enzyme catalysis and activation."
      Mehrotra S., Mylarappa B.N., Iyengar P., Balaram H.
      Biochim. Biophys. Acta 1804:1996-2002(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum."
      Eaazhisai K., Jayalakshmi R., Gayathri P., Anand R.P., Sumathy K., Balaram H., Murthy M.R.
      J. Mol. Biol. 335:1251-1264(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-442 IN COMPLEX WITH IMP; GDP; MAGNESIUM AND SUBSTRATE ANALOG.
      Strain: T9/106.

    Entry informationi

    Entry nameiPURA_PLAFA
    AccessioniPrimary (citable) accession number: Q9U8D3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: April 13, 2016
    This is version 82 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    Parasitic protozoa lack the de novo purine biosynthesis pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.