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O97069

- ASSY_DROME

UniProt

O97069 - ASSY_DROME

Protein

Argininosuccinate synthase

Gene

CG1315

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei86 – 861CitrullineBy similarity
    Binding sitei91 – 911CitrullineBy similarity
    Binding sitei118 – 1181AspartateBy similarity
    Binding sitei122 – 1221AspartateBy similarity
    Binding sitei122 – 1221CitrullineBy similarity
    Binding sitei123 – 1231AspartateBy similarity
    Binding sitei126 – 1261CitrullineBy similarity
    Binding sitei179 – 1791CitrullineBy similarity
    Binding sitei188 – 1881CitrullineBy similarity
    Binding sitei270 – 2701CitrullineBy similarity
    Binding sitei282 – 2821CitrullineBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 179ATPBy similarity
    Nucleotide bindingi114 – 1229ATPBy similarity

    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
    2. urea cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_210740. Urea cycle.
    UniPathwayiUPA00068; UER00113.
    UPA00158; UER00272.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Argininosuccinate synthase (EC:6.3.4.5)
    Alternative name(s):
    Citrulline--aspartate ligase
    Gene namesi
    ORF Names:CG1315
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0026565. CG1315.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Argininosuccinate synthasePRO_0000148557Add
    BLAST

    Proteomic databases

    PRIDEiO97069.

    Expressioni

    Gene expression databases

    BgeeiO97069.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi66010. 1 interaction.
    DIPiDIP-21101N.
    IntActiO97069. 1 interaction.
    MINTiMINT-958605.
    STRINGi7227.FBpp0081197.

    Structurei

    3D structure databases

    ProteinModelPortaliO97069.
    SMRiO97069. Positions 3-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0137.
    GeneTreeiENSGT00390000004524.
    InParanoidiO97069.
    KOiK01940.
    OMAiYKALAPH.
    OrthoDBiEOG7PVWPB.
    PhylomeDBiO97069.

    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.

    O97069-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKETVILAY SGGLDTSCVL KWLLDKQYEV ICVLADVGQK EDFTAAEKKA    50
    LKIGAKKVIV ADVKQSFVED YIWPAVQMGL VYEERYLLGT SLARPCISVA 100
    LMEVAREYGA KYLAHGATGK GNDQVRFELC AYALKPDLKI IAPWRDVEFC 150
    CQFQGRQDLI AYAQQHGIEV SAKPATPWST DANILHISYE SGILEDPNTV 200
    APENLYEMTV DPLTRAPRDP VHLVIQFDRG LPSSVEDLPG GRVYTKPLEM 250
    LDFLNKLGGS YGIGRIDIVE NRFVGLKSRG VYETPGGTIL FAAHQDLEVF 300
    ALDREVLRTK QVLRDRMADY VYNGFWFSPE AIYARKCIEL AEQRVSGKVT 350
    VELAPGYCRA IARKAAKDVG ALYNEQLVSM DVHGGYVPQD AGGFIAINAV 400
    RIREHVRAFG AYDVPTKKN 419
    Length:419
    Mass (Da):46,595
    Last modified:May 1, 1999 - v1
    Checksum:i0566A10A329BE513
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001572 Genomic DNA. Translation: AAD19816.1.
    AE014297 Genomic DNA. Translation: AAF54103.2.
    BT060440 mRNA. Translation: ACN22205.1.
    RefSeqiNP_001262324.1. NM_001275395.1.
    NP_649674.1. NM_141417.3.
    UniGeneiDm.20149.

    Genome annotation databases

    EnsemblMetazoaiFBtr0081699; FBpp0081197; FBgn0026565.
    GeneIDi40812.
    KEGGidme:Dmel_CG1315.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001572 Genomic DNA. Translation: AAD19816.1 .
    AE014297 Genomic DNA. Translation: AAF54103.2 .
    BT060440 mRNA. Translation: ACN22205.1 .
    RefSeqi NP_001262324.1. NM_001275395.1.
    NP_649674.1. NM_141417.3.
    UniGenei Dm.20149.

    3D structure databases

    ProteinModelPortali O97069.
    SMRi O97069. Positions 3-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66010. 1 interaction.
    DIPi DIP-21101N.
    IntActi O97069. 1 interaction.
    MINTi MINT-958605.
    STRINGi 7227.FBpp0081197.

    Proteomic databases

    PRIDEi O97069.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0081699 ; FBpp0081197 ; FBgn0026565 .
    GeneIDi 40812.
    KEGGi dme:Dmel_CG1315.

    Organism-specific databases

    FlyBasei FBgn0026565. CG1315.

    Phylogenomic databases

    eggNOGi COG0137.
    GeneTreei ENSGT00390000004524.
    InParanoidi O97069.
    KOi K01940.
    OMAi YKALAPH.
    OrthoDBi EOG7PVWPB.
    PhylomeDBi O97069.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    UPA00158 ; UER00272 .
    Reactomei REACT_210740. Urea cycle.

    Miscellaneous databases

    GenomeRNAii 40812.
    NextBioi 820710.
    PROi O97069.

    Gene expression databases

    Bgeei O97069.

    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 Antennapedia complex of Drosophila."
      Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., Palazzolo M.J.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Berkeley.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Carlson J.W., Booth B., Frise E., Sandler J., Wan K.H., Yu C., Celniker S.E.
      Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.

    Entry informationi

    Entry nameiASSY_DROME
    AccessioniPrimary (citable) accession number: O97069
    Secondary accession number(s): C0HDN4, Q9VI41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3