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P0A6E4

- ASSY_ECOLI

UniProt

P0A6E4 - ASSY_ECOLI

Protein

Argininosuccinate synthase

Gene

argG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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 sitei43 – 431ATP; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei99 – 991Citrulline2 Publications
    Binding sitei129 – 1291ATP; via amide nitrogen1 Publication
    Binding sitei131 – 1311Aspartate1 Publication
    Binding sitei131 – 1311ATP1 Publication
    Binding sitei135 – 1351Aspartate1 Publication
    Binding sitei135 – 1351Citrulline2 Publications
    Binding sitei136 – 1361Aspartate1 Publication
    Binding sitei136 – 1361ATP1 Publication
    Binding sitei139 – 1391Citrulline2 Publications
    Binding sitei192 – 1921Citrulline2 Publications
    Binding sitei194 – 1941ATP1 Publication
    Binding sitei201 – 2011Citrulline2 Publications
    Binding sitei203 – 2031Citrulline2 Publications
    Binding sitei280 – 2801Citrulline2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 259ATP1 Publication

    GO - Molecular functioni

    1. argininosuccinate synthase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP
    3. protein binding Source: IntAct

    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

    BioCyciEcoCyc:ARGSUCCINSYN-MONOMER.
    ECOL316407:JW3140-MONOMER.
    UniPathwayiUPA00068; UER00113.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Argininosuccinate synthase (EC:6.3.4.5)
    Alternative name(s):
    Citrulline--aspartate ligase
    Gene namesi
    Name:argG
    Ordered Locus Names:b3172, JW3140
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10068. argG.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 447446Argininosuccinate synthasePRO_0000148695Add
    BLAST

    Proteomic databases

    PaxDbiP0A6E4.
    PRIDEiP0A6E4.

    2D gel databases

    SWISS-2DPAGEP0A6E4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6E4.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dacBP242282EBI-1120296,EBI-1131834

    Protein-protein interaction databases

    DIPiDIP-35842N.
    IntActiP0A6E4. 13 interactions.
    STRINGi511145.b3172.

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Beta strandi12 – 176
    Helixi22 – 3312
    Beta strandi37 – 448
    Helixi55 – 639
    Beta strandi66 – 727
    Helixi74 – 8714
    Helixi102 – 12019
    Beta strandi125 – 1273
    Helixi136 – 14712
    Beta strandi152 – 1543
    Helixi156 – 1583
    Helixi160 – 1656
    Beta strandi166 – 1683
    Helixi169 – 17810
    Beta strandi190 – 1967
    Beta strandi199 – 2046
    Helixi205 – 2084
    Helixi214 – 2163
    Beta strandi220 – 2223
    Beta strandi235 – 2428
    Beta strandi245 – 2495
    Helixi257 – 26913
    Turni270 – 2745
    Beta strandi276 – 2816
    Beta strandi287 – 2937
    Helixi295 – 31117
    Helixi314 – 33219
    Helixi339 – 35113
    Helixi353 – 3553
    Beta strandi358 – 3647
    Beta strandi370 – 3767
    Turni384 – 3863
    Helixi398 – 4069
    Helixi409 – 42416
    Beta strandi427 – 4293
    Beta strandi433 – 4364

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K92X-ray1.60A2-447[»]
    1K97X-ray2.00A2-447[»]
    1KP2X-ray2.00A2-447[»]
    1KP3X-ray2.00A2-447[»]
    ProteinModelPortaliP0A6E4.
    SMRiP0A6E4. Positions 2-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6E4.

    Family & Domainsi

    Domaini

    The monomer is composed of two major structural domains: a nucleotide-binding domain and a catalytic/multimerization domain. Binding of ATP results in a large rigid body conformational change of the nucleotide binding domain.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0137.
    HOGENOMiHOG000230094.
    KOiK01940.
    OMAiRQEMSEF.
    OrthoDBiEOG6K9QCV.
    PhylomeDBiP0A6E4.

    Family and domain databases

    Gene3Di1.10.287.400. 1 hit.
    3.40.50.620. 1 hit.
    3.90.1260.10. 1 hit.
    HAMAPiMF_00581. Arg_succ_synth_type2.
    InterProiIPR023437. Arg_succ_synth_type2_subfam.
    IPR001518. Arginosuc_synth.
    IPR018223. Arginosuc_synth_CS.
    IPR024074. AS_cat/multimer_dom_body.
    IPR024073. AS_multimer_C_tail.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6E4-1 [UniParc]FASTAAdd to Basket

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    MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE    50
    EDYDAIPRRA MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF 100
    NTTPLGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLTNAE 150
    LQIYKPWLDT DFIDELGGRH EMSEFMIACG FDYKMSVEKA YSTDSNMLGA 200
    THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR FEQGHPVALN 250
    GKTFSDDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL 300
    HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR 350
    WVASQITGEV TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD 400
    RIGQLTMRNL DITDTREKLF GYAKTGLLSS SAASGVPQVE NLENKGQ 447
    Length:447
    Mass (Da):49,898
    Last modified:January 23, 2007 - v2
    Checksum:iD5E7E51BD06E1813
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti220 – 2201I → N in AAA23482. (PubMed:2123815)Curated
    Sequence conflicti328 – 3281G → D in AAA23482. (PubMed:2123815)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35236 Genomic DNA. Translation: AAA23482.1.
    U18997 Genomic DNA. Translation: AAA57974.1.
    U00096 Genomic DNA. Translation: AAC76205.1.
    AP009048 Genomic DNA. Translation: BAE77217.1.
    PIRiG65107. AJECRS.
    RefSeqiNP_417640.1. NC_000913.3.
    YP_491358.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76205; AAC76205; b3172.
    BAE77217; BAE77217; BAE77217.
    GeneIDi12934127.
    947590.
    KEGGiecj:Y75_p3093.
    eco:b3172.
    PATRICi32121762. VBIEscCol129921_3266.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35236 Genomic DNA. Translation: AAA23482.1 .
    U18997 Genomic DNA. Translation: AAA57974.1 .
    U00096 Genomic DNA. Translation: AAC76205.1 .
    AP009048 Genomic DNA. Translation: BAE77217.1 .
    PIRi G65107. AJECRS.
    RefSeqi NP_417640.1. NC_000913.3.
    YP_491358.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K92 X-ray 1.60 A 2-447 [» ]
    1K97 X-ray 2.00 A 2-447 [» ]
    1KP2 X-ray 2.00 A 2-447 [» ]
    1KP3 X-ray 2.00 A 2-447 [» ]
    ProteinModelPortali P0A6E4.
    SMRi P0A6E4. Positions 2-445.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35842N.
    IntActi P0A6E4. 13 interactions.
    STRINGi 511145.b3172.

    Chemistry

    DrugBanki DB00536. Guanidine.

    2D gel databases

    SWISS-2DPAGE P0A6E4.

    Proteomic databases

    PaxDbi P0A6E4.
    PRIDEi P0A6E4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76205 ; AAC76205 ; b3172 .
    BAE77217 ; BAE77217 ; BAE77217 .
    GeneIDi 12934127.
    947590.
    KEGGi ecj:Y75_p3093.
    eco:b3172.
    PATRICi 32121762. VBIEscCol129921_3266.

    Organism-specific databases

    EchoBASEi EB0066.
    EcoGenei EG10068. argG.

    Phylogenomic databases

    eggNOGi COG0137.
    HOGENOMi HOG000230094.
    KOi K01940.
    OMAi RQEMSEF.
    OrthoDBi EOG6K9QCV.
    PhylomeDBi P0A6E4.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci EcoCyc:ARGSUCCINSYN-MONOMER.
    ECOL316407:JW3140-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6E4.
    PROi P0A6E4.

    Gene expression databases

    Genevestigatori P0A6E4.

    Family and domain databases

    Gene3Di 1.10.287.400. 1 hit.
    3.40.50.620. 1 hit.
    3.90.1260.10. 1 hit.
    HAMAPi MF_00581. Arg_succ_synth_type2.
    InterProi IPR023437. Arg_succ_synth_type2_subfam.
    IPR001518. Arginosuc_synth.
    IPR018223. Arginosuc_synth_CS.
    IPR024074. AS_cat/multimer_dom_body.
    IPR024073. AS_multimer_C_tail.
    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. "Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals."
      van Vliet F., Crabeel M., Boyen A., Tricot C., Stalon V., Falmagne P., Nakamura Y., Baumberg S., Glansdorff N.
      Gene 95:99-104(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    5. "Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase."
      Lemke C., Yeung M., Howell P.L.
      Acta Crystallogr. D 55:2028-2030(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, CRYSTALLIZATION.
    6. "The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis."
      Lemke C.T., Howell P.L.
      Structure 9:1153-1164(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) UNCOMPLEXED AND IN COMPLEX WITH ASPARTATE AND CITRULLINE.
    7. "Substrate induced conformational changes in argininosuccinate synthetase."
      Lemke C.T., Howell P.L.
      J. Biol. Chem. 277:13074-13081(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP AND CITRULLINE.

    Entry informationi

    Entry nameiASSY_ECOLI
    AccessioniPrimary (citable) accession number: P0A6E4
    Secondary accession number(s): P22767, Q2M939
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 93 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3