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A5ILL1

- ASSY_THEP1

UniProt

A5ILL1 - ASSY_THEP1

Protein

Argininosuccinate synthase

Gene

argG

Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (26 Jun 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 sitei34 – 341ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
    Binding sitei85 – 851CitrullineUniRule annotation
    Binding sitei115 – 1151ATP; via amide nitrogenUniRule annotation
    Binding sitei117 – 1171AspartateUniRule annotation
    Binding sitei121 – 1211AspartateUniRule annotation
    Binding sitei121 – 1211CitrullineUniRule annotation
    Binding sitei122 – 1221AspartateUniRule annotation
    Binding sitei125 – 1251CitrullineUniRule annotation
    Binding sitei178 – 1781CitrullineUniRule annotation
    Binding sitei187 – 1871CitrullineUniRule annotation
    Binding sitei268 – 2681CitrullineUniRule annotation
    Binding sitei280 – 2801CitrullineUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi8 – 169ATPUniRule 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

    BioCyciTPET390874:GHJI-1099-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:Tpet_1067
    OrganismiThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
    Taxonomic identifieri390874 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000006558: 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 – 409409Argininosuccinate synthasePRO_1000000445Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi390874.Tpet_1067.

    Structurei

    3D structure databases

    ProteinModelPortaliA5ILL1.
    SMRiA5ILL1. Positions 2-404.
    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.

    A5ILL1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFDAIKEKAL    50
    KTGASKVYVE DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ 100
    VEIAEKEGAQ YVAHGATGKG NDQVRFELTY AALNPNLKVI SPWKDPEFLA 150
    KFKGRTDLIN YAMEKGIPIK VSKKRPYSED ENLMHISHEA GKLEDPAYIP 200
    DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT EKTDPLELFE 250
    YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM 300
    DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS 350
    IYKGNVMPVA RYSPYSLYNP ELSSMDVEGG FNATDSKGFI NIHALRLKVH 400
    QLVKKGYQK 409
    Length:409
    Mass (Da):46,067
    Last modified:June 26, 2007 - v1
    Checksum:iE3EC6EDF6BB2C42F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000702 Genomic DNA. Translation: ABQ47084.1.
    RefSeqiYP_001244660.1. NC_009486.1.

    Genome annotation databases

    EnsemblBacteriaiABQ47084; ABQ47084; Tpet_1067.
    GeneIDi5171371.
    KEGGitpt:Tpet_1067.
    PATRICi23944936. VBIThePet65348_1079.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000702 Genomic DNA. Translation: ABQ47084.1 .
    RefSeqi YP_001244660.1. NC_009486.1.

    3D structure databases

    ProteinModelPortali A5ILL1.
    SMRi A5ILL1. Positions 2-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 390874.Tpet_1067.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ47084 ; ABQ47084 ; Tpet_1067 .
    GeneIDi 5171371.
    KEGGi tpt:Tpet_1067.
    PATRICi 23944936. VBIThePet65348_1079.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci TPET390874:GHJI-1099-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

    Entry informationi

    Entry nameiASSY_THEP1
    AccessioniPrimary (citable) accession number: A5ILL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 49 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

    Documents

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

    External Data

    Dasty 3