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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 (ASL), Adenylosuccinate lyase (adsl), Adenylosuccinate lyase (adsl), 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)DescriptionActionsGraphical viewLength
    Active sitei26Proton acceptorUniRule annotation1
    Metal bindingi26MagnesiumUniRule annotation1
    Metal bindingi53Magnesium; via carbonyl oxygenUniRule annotation1
    Active sitei54Proton donorUniRule annotation1
    Binding sitei62GTPUniRule annotation1
    Binding sitei141IMPUniRule annotation1
    Binding sitei155IMP; shared with dimeric partnerUniRule annotation1
    Binding sitei232IMPUniRule annotation1
    Binding sitei247IMPUniRule annotation1
    Binding sitei307GTPUniRule annotation1
    Binding sitei311IMPUniRule annotation1
    Binding sitei313GTPUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi25 – 31GTPUniRule annotation7
    Nucleotide bindingi53 – 55GTPUniRule annotation3
    Nucleotide bindingi339 – 341GTPUniRule annotation3
    Nucleotide bindingi425 – 427GTPUniRule annotation3

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00003992941 – 442Adenylosuccinate synthetaseAdd BLAST442

    Proteomic databases

    PaxDbiQ9U8D3.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi5833.PF13_0287.

    Structurei

    Secondary structure

    1442
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi16 – 25Combined sources10
    Helixi29 – 36Combined sources8
    Helixi37 – 39Combined sources3
    Beta strandi41 – 45Combined sources5
    Beta strandi54 – 58Combined sources5
    Beta strandi61 – 68Combined sources8
    Turni70 – 73Combined sources4
    Beta strandi78 – 81Combined sources4
    Helixi89 – 99Combined sources11
    Helixi103 – 106Combined sources4
    Beta strandi107 – 110Combined sources4
    Beta strandi113 – 115Combined sources3
    Helixi118 – 133Combined sources16
    Beta strandi142 – 144Combined sources3
    Helixi145 – 153Combined sources9
    Helixi160 – 164Combined sources5
    Helixi166 – 183Combined sources18
    Helixi191 – 205Combined sources15
    Helixi206 – 208Combined sources3
    Helixi212 – 221Combined sources10
    Beta strandi226 – 229Combined sources4
    Helixi234 – 236Combined sources3
    Turni238 – 240Combined sources3
    Helixi253 – 258Combined sources6
    Turni259 – 261Combined sources3
    Helixi264 – 266Combined sources3
    Beta strandi269 – 280Combined sources12
    Beta strandi282 – 284Combined sources3
    Helixi293 – 301Combined sources9
    Turni307 – 309Combined sources3
    Beta strandi314 – 316Combined sources3
    Helixi320 – 330Combined sources11
    Beta strandi333 – 338Combined sources6
    Helixi340 – 343Combined sources4
    Beta strandi347 – 357Combined sources11
    Turni358 – 360Combined sources3
    Helixi373 – 376Combined sources4
    Beta strandi379 – 387Combined sources9
    Helixi399 – 401Combined sources3
    Helixi404 – 417Combined sources14
    Beta strandi421 – 425Combined sources5
    Beta strandi427 – 429Combined sources3
    Beta strandi433 – 435Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1P9BX-ray2.00A3-442[»]
    ProteinModelPortaliQ9U8D3.
    SMRiQ9U8D3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9U8D3.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni26 – 29IMP bindingUniRule annotation4
    Regioni51 – 54IMP bindingUniRule annotation4
    Regioni307 – 313Substrate bindingUniRule annotation7

    Sequence similaritiesi

    Belongs to the adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiKOG1355. Eukaryota.
    COG0104. LUCA.

    Family and domain databases

    CDDicd03108. AdSS. 1 hit.
    HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1P9BX-ray2.00A3-442[»]
    ProteinModelPortaliQ9U8D3.
    SMRiQ9U8D3.
    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

    CDDicd03108. AdSS. 1 hit.
    HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
    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...

    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: November 2, 2016
    This is version 85 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.