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Q3SHT1

- ASSY_THIDA

UniProt

Q3SHT1 - ASSY_THIDA

Protein

Argininosuccinate synthase

Gene

argG

Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 2 (12 Dec 2006)
      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 sitei37 – 371ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
    Binding sitei90 – 901CitrullineUniRule annotation
    Binding sitei95 – 951CitrullineUniRule annotation
    Binding sitei120 – 1201ATP; via amide nitrogenUniRule annotation
    Binding sitei122 – 1221AspartateUniRule annotation
    Binding sitei126 – 1261AspartateUniRule annotation
    Binding sitei126 – 1261CitrullineUniRule annotation
    Binding sitei127 – 1271AspartateUniRule annotation
    Binding sitei130 – 1301CitrullineUniRule annotation
    Binding sitei182 – 1821CitrullineUniRule annotation
    Binding sitei191 – 1911CitrullineUniRule annotation
    Binding sitei267 – 2671CitrullineUniRule annotation
    Binding sitei279 – 2791CitrullineUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATPUniRule 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

    BioCyciTDEN292415:GHWG-1892-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:Tbd_1849
    OrganismiThiobacillus denitrificans (strain ATCC 25259)
    Taxonomic identifieri292415 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
    ProteomesiUP000008291: 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_0000263989Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi292415.Tbd_1849.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3SHT1.
    SMRiQ3SHT1. Positions 6-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0137.
    HOGENOMiHOG000230093.
    KOiK01940.
    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.

    Q3SHT1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDIKKVVLA YSGGLDTSVI LKWLQDTYQC EVVTFTADLG QGEELEPARQ    50
    KALQFGIKPE QIYIDDLREE FVRDFVFPMF RANTVYEGEY LLGTSIARPL 100
    IAKRLIEIVN ATGADAICHG ATGKGNDQVR FELGAYALKP DVKVIAPWRE 150
    WDLLSREKLL AYAESHGIPI DMKHRQGGSP YSMDANLLHI SYEGRHLEDP 200
    SAEAEEDMWR WTVSPEKAPD AAEYIELTYA KGDVVAIDGQ QMPAHEVLAK 250
    LNELGGKHGI GRLDLVENRY VGMKSRGCYE TPGGTILLKA HRAIESITLD 300
    REVAHLKDDL MPRYASLIYN GYWWAPERRA LQVLIDHTQA HVNGTVRLKL 350
    YKGNVIVVGR DSKNDSLFDS TIATFEDDAG AYDQKDAGGF IKLNALRMRI 400
    AAKLDARRK 409
    Length:409
    Mass (Da):45,869
    Last modified:December 12, 2006 - v2
    Checksum:i687B28A5080F0175
    GO

    Sequence cautioni

    The sequence AAZ97802.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000116 Genomic DNA. Translation: AAZ97802.1. Different initiation.
    RefSeqiYP_315607.2. NC_007404.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ97802; AAZ97802; Tbd_1849.
    GeneIDi3671514.
    KEGGitbd:Tbd_1849.
    PATRICi23969867. VBIThiDen82923_1827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000116 Genomic DNA. Translation: AAZ97802.1 . Different initiation.
    RefSeqi YP_315607.2. NC_007404.1.

    3D structure databases

    ProteinModelPortali Q3SHT1.
    SMRi Q3SHT1. Positions 6-402.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 292415.Tbd_1849.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ97802 ; AAZ97802 ; Tbd_1849 .
    GeneIDi 3671514.
    KEGGi tbd:Tbd_1849.
    PATRICi 23969867. VBIThiDen82923_1827.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci TDEN292415:GHWG-1892-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. "The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
      Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
      J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25259.

    Entry informationi

    Entry nameiASSY_THIDA
    AccessioniPrimary (citable) accession number: Q3SHT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 60 of the entry and version 2 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