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A1ATU4

- ASSY_PELPD

UniProt

A1ATU4 - ASSY_PELPD

Protein

Argininosuccinate synthase

Gene

argG

Organism
Pelobacter propionicus (strain DSM 2379)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
    Binding sitei92 – 921CitrullineUniRule annotation
    Binding sitei97 – 971CitrullineUniRule annotation
    Binding sitei122 – 1221ATP; via amide nitrogenUniRule annotation
    Binding sitei124 – 1241AspartateUniRule annotation
    Binding sitei128 – 1281AspartateUniRule annotation
    Binding sitei128 – 1281CitrullineUniRule annotation
    Binding sitei129 – 1291AspartateUniRule annotation
    Binding sitei132 – 1321CitrullineUniRule annotation
    Binding sitei181 – 1811CitrullineUniRule annotation
    Binding sitei190 – 1901CitrullineUniRule annotation
    Binding sitei266 – 2661CitrullineUniRule annotation
    Binding sitei278 – 2781CitrullineUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 229ATPUniRule annotation

    GO - Molecular functioni

    1. argininosuccinate synthase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. arginine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPPRO338966:GHL0-3228-MONOMER.
    UniPathwayiUPA00068; UER00113.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Argininosuccinate synthaseUniRule annotation (EC:6.3.4.5UniRule annotation)
    Alternative name(s):
    Citrulline--aspartate ligaseUniRule annotation
    Gene namesi
    Name:argGUniRule annotation
    Ordered Locus Names:Ppro_3171
    OrganismiPelobacter propionicus (strain DSM 2379)
    Taxonomic identifieri338966 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
    ProteomesiUP000006732: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 408408Argininosuccinate synthasePRO_1000000416Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi338966.Ppro_3171.

    Structurei

    3D structure databases

    ProteinModelPortaliA1ATU4.
    SMRiA1ATU4. Positions 11-403.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the argininosuccinate synthase family. Type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0137.
    HOGENOMiHOG000230093.
    KOiK01940.
    OMAiAPPEEAY.
    OrthoDBiEOG6K9QCV.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.90.1260.10. 1 hit.
    HAMAPiMF_00005. Arg_succ_synth_type1.
    InterProiIPR001518. Arginosuc_synth.
    IPR018223. Arginosuc_synth_CS.
    IPR023434. Arginosuc_synth_type_1_subfam.
    IPR024074. AS_cat/multimer_dom_body.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00764. Arginosuc_synth. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00032. argG. 1 hit.
    PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
    PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1ATU4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQQKMDIKN VVLAYSGGLD TSIILKWLKN EYGCRVVAFS ADLGQGEELD    50
    PVREKALATG ADVVYIDDLR EEFVRDFVFP MFRANAIYEG HYLLGTSIAR 100
    PLIAKRQMEI AAKEGCDAVS HGSTGKGNDQ VRFELGYYHF NPNIKIVAPW 150
    RTWDLNSRQA LIDYAKKNGI PVPVTKKRPW SSDRNLLHIS FEGGILEDTW 200
    AEAPEEMYVL TTAPEKAPNK PQYVEIEFKN GNAVAVDGEK MTPAQLLAHL 250
    NYLGGQHGIG RVDLLENRSV GMKSRGVYET PGGTILREAH MAVEQITMDR 300
    EVMRIRDGLI PEYARLVYAG YWFSPEREML QALIDDSQKC VNGVARLKLY 350
    KGYCRTVGRK SDTDSLFNQD FATFEKDQVY NQADAEGFIR INSLRLRIRS 400
    MMQAAKKK 408
    Length:408
    Mass (Da):46,135
    Last modified:January 23, 2007 - v1
    Checksum:iA2EF9B029764DF1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000482 Genomic DNA. Translation: ABL00765.1.
    RefSeqiYP_902822.1. NC_008609.1.

    Genome annotation databases

    EnsemblBacteriaiABL00765; ABL00765; Ppro_3171.
    GeneIDi4573273.
    KEGGippd:Ppro_3171.
    PATRICi22899483. VBIPelPro64470_3328.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000482 Genomic DNA. Translation: ABL00765.1 .
    RefSeqi YP_902822.1. NC_008609.1.

    3D structure databases

    ProteinModelPortali A1ATU4.
    SMRi A1ATU4. Positions 11-403.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 338966.Ppro_3171.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL00765 ; ABL00765 ; Ppro_3171 .
    GeneIDi 4573273.
    KEGGi ppd:Ppro_3171.
    PATRICi 22899483. VBIPelPro64470_3328.

    Phylogenomic databases

    eggNOGi COG0137.
    HOGENOMi HOG000230093.
    KOi K01940.
    OMAi APPEEAY.
    OrthoDBi EOG6K9QCV.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci PPRO338966:GHL0-3228-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.90.1260.10. 1 hit.
    HAMAPi MF_00005. Arg_succ_synth_type1.
    InterProi IPR001518. Arginosuc_synth.
    IPR018223. Arginosuc_synth_CS.
    IPR023434. Arginosuc_synth_type_1_subfam.
    IPR024074. AS_cat/multimer_dom_body.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00764. Arginosuc_synth. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00032. argG. 1 hit.
    PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
    PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
      , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2379.

    Entry informationi

    Entry nameiASSY_PELPD
    AccessioniPrimary (citable) accession number: A1ATU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 47 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3