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A0LE34

- ASSY_MAGSM

UniProt

A0LE34 - ASSY_MAGSM

Protein

Argininosuccinate synthase

Gene

argG

Organism
Magnetococcus sp. (strain MC-1)
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 (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 sitei38 – 381ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
    Binding sitei89 – 891CitrullineUniRule annotation
    Binding sitei94 – 941CitrullineUniRule annotation
    Binding sitei119 – 1191ATP; via amide nitrogenUniRule annotation
    Binding sitei121 – 1211AspartateUniRule annotation
    Binding sitei125 – 1251AspartateUniRule annotation
    Binding sitei125 – 1251CitrullineUniRule annotation
    Binding sitei126 – 1261AspartateUniRule annotation
    Binding sitei129 – 1291CitrullineUniRule annotation
    Binding sitei180 – 1801CitrullineUniRule annotation
    Binding sitei189 – 1891CitrullineUniRule annotation
    Binding sitei265 – 2651CitrullineUniRule annotation
    Binding sitei277 – 2771CitrullineUniRule 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

    BioCyciMSP156889:GH36-3797-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:Mmc1_3742
    OrganismiMagnetococcus sp. (strain MC-1)
    Taxonomic identifieri156889 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
    ProteomesiUP000002586: 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 – 407407Argininosuccinate synthasePRO_1000057040Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi156889.Mmc1_3742.

    Structurei

    3D structure databases

    ProteinModelPortaliA0LE34.
    SMRiA0LE34. Positions 7-401.
    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.

    A0LE34-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNGIDKVVL AYSGGLDTSI ILKWLQDEYQ CEVVAFCADL GQAEELEPAR    50
    AKAEKFGVKE IYIDDLKEEF VRDFVFPMYR ANTLYEGVYH LGTSIARPLI 100
    AKRQIEIANA TGAQAVSHGA TGKGNDQVRF ELGYYALRPD IRVIAPWREW 150
    DLTSRDKLFA YAEKHGIPVP TDKRGEVPYS MDRNLLHISF EGKALEDPWV 200
    EPDEEMFVLS VSPEKAPDQA TYVELTFRQG DLVAIDDQEM SPATLLAKLN 250
    QLGGRNGIGR LDLVENRYVG MKSRGVYETP GGTILGVAHR AMESLTLDRE 300
    VAHMKDELMP RYAKLIYNGY WFSPERAMLQ TMIDASQTFV NGKVRVKLYK 350
    GNVVVVGRQS ENSLFDPAIA TFEDDKGAYN QADADGFIKL NALRMRIAAM 400
    LRNGPKV 407
    Length:407
    Mass (Da):45,648
    Last modified:December 12, 2006 - v1
    Checksum:i6A1864EC9BCE2E68
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK46227.1.
    RefSeqiYP_867633.1. NC_008576.1.

    Genome annotation databases

    EnsemblBacteriaiABK46227; ABK46227; Mmc1_3742.
    GeneIDi4483400.
    KEGGimgm:Mmc1_3742.
    PATRICi22434223. VBIMagSp23654_3829.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK46227.1 .
    RefSeqi YP_867633.1. NC_008576.1.

    3D structure databases

    ProteinModelPortali A0LE34.
    SMRi A0LE34. Positions 7-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 156889.Mmc1_3742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK46227 ; ABK46227 ; Mmc1_3742 .
    GeneIDi 4483400.
    KEGGi mgm:Mmc1_3742.
    PATRICi 22434223. VBIMagSp23654_3829.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci MSP156889:GH36-3797-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: MC-1.

    Entry informationi

    Entry nameiASSY_MAGSM
    AccessioniPrimary (citable) accession number: A0LE34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: December 12, 2006
    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, 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