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Q9K4Y8

- ASSY_MORAB

UniProt

Q9K4Y8 - ASSY_MORAB

Protein

Argininosuccinate synthase

Gene

argG

Organism
Moritella abyssi
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 sitei40 – 401ATP; 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 bindingi11 – 199ATPUniRule 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

    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
    OrganismiMoritella abyssi
    Taxonomic identifieri111292 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

    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 – 404404Argininosuccinate synthasePRO_0000148612Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ9K4Y8.
    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: Complete.

    Q9K4Y8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQTVKKVVV AYSGGLDTSV ILPWLQENYD NCEIVALFVA DVGQGAEELE    50
    GIEAKALASG ASECYVVDLK DELVENYIYP TLKTGAVYEG TYLLGTSMAR 100
    QSIAKAQVEI ARKVGADALC HGCTGKGNDQ IRFESCFAAL APELTVIAPW 150
    RIWDLTSRES LLEYLAERDI PTAASGTKIY SRDANAWHIS HEGGELEDPW 200
    NQPSKQVWTM TVDPIDAPNE PEFLTISVVK GEITAVNGEE MYLIIRYTYL 250
    NEKAAAHGVG RVDIVENRLV GMKSRGCYET PGGTVMVEAL RGIEELVLDK 300
    ITRKWKHTVA AEFSHLVYDG RWFTPLCASL LAAAGTLAEE MNGEVIVKMY 350
    KGSVQAVQKQ SPNSLYSEEF ATFGDDNVYD DQSHAEGFIR LYSLSSRIKA 400
    LASK 404
    Length:404
    Mass (Da):44,432
    Last modified:October 1, 2000 - v1
    Checksum:i9E1C4D037AF5923F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ252021 Genomic DNA. Translation: CAB95023.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ252021 Genomic DNA. Translation: CAB95023.1 .

    3D structure databases

    ProteinModelPortali Q9K4Y8.
    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. "Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase."
      Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.
      J. Bacteriol. 182:1609-1615(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 2693.

    Entry informationi

    Entry nameiASSY_MORAB
    AccessioniPrimary (citable) accession number: Q9K4Y8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 66 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