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Q8GDU2

- ASSY_HELMO

UniProt

Q8GDU2 - ASSY_HELMO

Protein

Argininosuccinate synthase

Gene

argG

Organism
Heliobacillus mobilis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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-EC
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    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
    OrganismiHeliobacillus mobilis
    Taxonomic identifieri28064 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacillus

    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 – ›408›408Argininosuccinate synthasePRO_0000148598Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ8GDU2.
    SMRiQ8GDU2. Positions 10-403.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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: Fragment.

    Q8GDU2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGALGMSKK VVLAYSGGLD TSIIIPWLKE NYGYEVIAMA ADLGQGEELE    50
    PLNEKAINTG ATKIYIEDVK EEFVTEFIWP TLKAGAVYEG KYLLGTSFAR 100
    PLIAKRLVEI ARKEGAEAIA HGATGKGNDQ VRFELTVKAL APDLKIVAPW 150
    REWDIRSRED AIDYAQARNI PVPVKKDRPY SMDRNLWHLS HEGADLESPW 200
    NEPQNDLFMI CTPPEQAPDK PEYVEIEFEK GIPVKLNGEA LGPVEMIEKL 250
    NAIAAAHGVG ICDMVENRLV GMKSRGVYET PAGTVLYAAH RELEYLCLDR 300
    ATMHYKEMVA LRYAELVYDG VWYHPLRKAI DAFVDVTQET VTGLVRMKLF 350
    KGSVTPAGAK SPYSLYNEEF STFGRDEVYN QKDAEGFINL FGLPMKVRAL 400
    MEQKSGLK 408
    Length:408
    Mass (Da):45,642
    Last modified:March 1, 2003 - v1
    Checksum:i9B4DEC08F0640542
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei408 – 4081

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY142882 Genomic DNA. Translation: AAN87486.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY142882 Genomic DNA. Translation: AAN87486.1 .

    3D structure databases

    ProteinModelPortali Q8GDU2.
    SMRi Q8GDU2. Positions 10-403.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .

    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 [GENOMIC DNA].

    Entry informationi

    Entry nameiASSY_HELMO
    AccessioniPrimary (citable) accession number: Q8GDU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3