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A6UE09

- ASSY_SINMW

UniProt

A6UE09 - ASSY_SINMW

Protein

Argininosuccinate synthase

Gene

argG

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      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 sitei91 – 911CitrullineUniRule annotation
    Binding sitei96 – 961CitrullineUniRule annotation
    Binding sitei121 – 1211ATP; via amide nitrogenUniRule annotation
    Binding sitei123 – 1231AspartateUniRule annotation
    Binding sitei127 – 1271AspartateUniRule annotation
    Binding sitei127 – 1271CitrullineUniRule annotation
    Binding sitei128 – 1281AspartateUniRule annotation
    Binding sitei131 – 1311CitrullineUniRule 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 bindingi13 – 219ATPUniRule 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

    BioCyciSMED366394:GJAL-3115-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:Smed_3063
    OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
    Taxonomic identifieri366394 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000001108: 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 – 405405Argininosuccinate synthasePRO_1000000437Add
    BLAST

    Proteomic databases

    ProMEXiA6UE09.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi366394.Smed_3063.

    Structurei

    3D structure databases

    ProteinModelPortaliA6UE09.
    SMRiA6UE09. Positions 9-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0137.
    HOGENOMiHOG000230093.
    KOiK01940.
    OMAiVEEYIWR.
    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.

    A6UE09-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASHKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP    50
    ARKKAEMLGI KEIYIEDVRE EFVKDFVFPM FRANAVYEGV YLLGTSIARP 100
    LISKHLIDIA RKTGADAIAH GATGKGNDQV RFELSAYALN PDIKIIAPWR 150
    DWSFKSRTDL LEFAEKHQIP VAKDKKGEAP FSVDANLLHS SSEGKVLEDP 200
    AQEAPEYVHM RTISPEAAPD KATIIKVGFE RGDAVSIDGV RMSAATLLAK 250
    LNEYGRDNGI GRLDLVENRF VGMKSRGVYE TPGGTILLSA HRAIESITLD 300
    RGAAHLKDEL MPRYAELIYY GFWFSPEREM LQAAIDKSQE HVEGEVTLKL 350
    YKGNVMVVGR ESGKSLYSDK LVTFEDDQGA YDQKDAAGFI KLNALRLRTL 400
    AARNR 405
    Length:405
    Mass (Da):44,937
    Last modified:August 21, 2007 - v1
    Checksum:i1F9ECA9A883459A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000738 Genomic DNA. Translation: ABR61889.1.
    RefSeqiYP_001328724.1. NC_009636.1.

    Genome annotation databases

    EnsemblBacteriaiABR61889; ABR61889; Smed_3063.
    GeneIDi5323942.
    KEGGismd:Smed_3063.
    PATRICi23625351. VBISinMed134228_6293.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000738 Genomic DNA. Translation: ABR61889.1 .
    RefSeqi YP_001328724.1. NC_009636.1.

    3D structure databases

    ProteinModelPortali A6UE09.
    SMRi A6UE09. Positions 9-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 366394.Smed_3063.

    Proteomic databases

    ProMEXi A6UE09.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR61889 ; ABR61889 ; Smed_3063 .
    GeneIDi 5323942.
    KEGGi smd:Smed_3063.
    PATRICi 23625351. VBISinMed134228_6293.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci SMED366394:GJAL-3115-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 Sinorhizobium medicae WSM419 chromosome."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WSM419.

    Entry informationi

    Entry nameiASSY_SINMW
    AccessioniPrimary (citable) accession number: A6UE09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 46 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

    Documents

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

    External Data

    Dasty 3