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Q2RMV0

- ASSY_RHORT

UniProt

Q2RMV0 - ASSY_RHORT

Protein

Argininosuccinate synthase

Gene

argG

Organism
Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (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 sitei39 – 391ATP; 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 sitei181 – 1811CitrullineUniRule annotation
    Binding sitei190 – 1901CitrullineUniRule annotation
    Binding sitei266 – 2661CitrullineUniRule annotation
    Binding sitei278 – 2781CitrullineUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 209ATPUniRule 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

    BioCyciRRUB269796:GCN1-3816-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:Rru_A3751
    OrganismiRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)
    Taxonomic identifieri269796 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
    ProteomesiUP000001929: 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 – 404404Argininosuccinate synthasePRO_0000263965Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi269796.Rru_A3751.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2RMV0.
    SMRiQ2RMV0. Positions 8-397.
    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.

    Q2RMV0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKGDVKKVV LAYSGGLDTS IILRWLQDEY DCEVVTFTAD IGQGEELEPA    50
    RQKAEMMGIK EIYIEDLREE FVRDYVFPMF RANTLYEGVY LLGTSIARPL 100
    IGKRLVEIAE ATGADAVSHG ATGKGNDQVR FELTAYALKP DIKIIAPWRT 150
    WDLHSRTKLI EYAMRHQIPV PKDKHGEAPY SMDANLLHIS YEGKALENPW 200
    TEPSEDMFRL TVSPEAAPDK AQYIEVDFER GDAVAIDGEK LTPAALLAKL 250
    NEIGGRHGVG RLDLVENRYV GMKSRGVYET PGGTILQVAH RAVESLTLDR 300
    EVMHLRDELM PRYAKLIYNG FWFAPERLML QAAIDQTQQT VTGTARLKLY 350
    KGNVSVVGRK AAKSLYRMDY VTFEEDTVYD QHDAEGFIKL NALRLRLGKM 400
    ARDS 404
    Length:404
    Mass (Da):45,609
    Last modified:December 12, 2006 - v2
    Checksum:iC48350F8AC1AE4CB
    GO

    Sequence cautioni

    The sequence ABC24545.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000230 Genomic DNA. Translation: ABC24545.1. Different initiation.
    RefSeqiYP_428832.1. NC_007643.1.

    Genome annotation databases

    EnsemblBacteriaiABC24545; ABC24545; Rru_A3751.
    GeneIDi3837208.
    KEGGirru:Rru_A3751.
    PATRICi23331318. VBIRhoRub82919_3875.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000230 Genomic DNA. Translation: ABC24545.1 . Different initiation.
    RefSeqi YP_428832.1. NC_007643.1.

    3D structure databases

    ProteinModelPortali Q2RMV0.
    SMRi Q2RMV0. Positions 8-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269796.Rru_A3751.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC24545 ; ABC24545 ; Rru_A3751 .
    GeneIDi 3837208.
    KEGGi rru:Rru_A3751.
    PATRICi 23331318. VBIRhoRub82919_3875.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci RRUB269796:GCN1-3816-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. "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
      , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

    Entry informationi

    Entry nameiASSY_RHORT
    AccessioniPrimary (citable) accession number: Q2RMV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 57 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