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P22768

- ASSY_YEAST

UniProt

P22768 - ASSY_YEAST

Protein

Argininosuccinate synthase

Gene

ARG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the eighth step in arginine biosynthesis. Also has a catabolic function as the first enzyme of citrulline utilization as nitrogen source via arginine and the reactions involved in the arginase pathway.1 Publication

    Catalytic activityi

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

    Kineticsi

    1. KM=0.1 mM for L-citrulline1 Publication
    2. KM=0.03 mM for L-aspartate1 Publication
    3. KM=0.3 mM for ATP1 Publication

    pH dependencei

    Optimum pH is 7.5-8.0 for the forward reaction and 6.0-6.5 for the reverse reaction.1 Publication

    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 sitei273 – 2731CitrullineBy similarity
    Binding sitei285 – 2851CitrullineBy similarity

    Regions

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

    GO - Molecular functioni

    1. argininosuccinate synthase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YOL058W-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:ARG1
    Ordered Locus Names:YOL058W
    ORF Names:O1228
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL058w.
    SGDiS000005419. ARG1.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytosol Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Argininosuccinate synthasePRO_0000148559Add
    BLAST

    Proteomic databases

    MaxQBiP22768.
    PaxDbiP22768.
    PeptideAtlasiP22768.

    Expressioni

    Gene expression databases

    GenevestigatoriP22768.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi34343. 17 interactions.
    DIPiDIP-1660N.
    IntActiP22768. 4 interactions.
    MINTiMINT-393127.
    STRINGi4932.YOL058W.

    Structurei

    3D structure databases

    ProteinModelPortaliP22768.
    SMRiP22768. Positions 3-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0137.
    GeneTreeiENSGT00390000004524.
    HOGENOMiHOG000230093.
    KOiK01940.
    OMAiPECEYIR.
    OrthoDBiEOG7KSXJR.

    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.

    P22768-1 [UniParc]FASTAAdd to Basket

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    MSKGKVCLAY SGGLDTSVIL AWLLDQGYEV VAFMANVGQE EDFDAAKEKA    50
    LKIGACKFVC VDCREDFVKD ILFPAVQVNA VYEDVYLLGT SLARPVIAKA 100
    QIDVAKQEGC FAVSHGCTGK GNDQIRFELS FYALKPDVKC ITPWRMPEFF 150
    ERFAGRKDLL DYAAQKGIPV AQTKAKPWST DENQAHISYE AGILEDPDTT 200
    PPKDMWKLIV DPMDAPDQPQ DLTIDFERGL PVKLTYTDNK TSKEVSVTKP 250
    LDVFLAASNL ARANGVGRID IVEDRYINLK SRGCYEQAPL TVLRKAHVDL 300
    EGLTLDKEVR QLRDSFVTPN YSRLIYNGSY FTPECEYIRS MIQPSQNSVN 350
    GTVRVRLYKG NVIILGRSTK TEKLYDPTES SMDELTGFLP TDTTGFIAIQ 400
    AIRIKKYGES KKTKGEELTL 420
    Length:420
    Mass (Da):46,928
    Last modified:September 21, 2011 - v3
    Checksum:i155E1A4775B6FA9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 282GY → AT in AAA34437. (PubMed:2123815)Curated
    Sequence conflicti27 – 282GY → AT in CAA30106. (PubMed:2897249)Curated
    Sequence conflicti48 – 492EK → VL in AAA34437. (PubMed:2123815)Curated
    Sequence conflicti48 – 492EK → VL in CAA30106. (PubMed:2897249)Curated
    Sequence conflicti61 – 644VDCR → GGLS in AAA34437. (PubMed:2123815)Curated
    Sequence conflicti169 – 1691P → F in AAA34437. (PubMed:2123815)Curated
    Sequence conflicti316 – 3161F → L in AAA34437. (PubMed:2123815)Curated
    Sequence conflicti329 – 3324SYFT → FLLH in AAA34437. (PubMed:2123815)Curated
    Sequence conflicti329 – 3324SYFT → FLLH in CAA62528. (PubMed:8789261)Curated
    Sequence conflicti329 – 3324SYFT → FLLH in CAA99067. (PubMed:9169874)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35237 Genomic DNA. Translation: AAA34437.1.
    X91067 Genomic DNA. Translation: CAA62528.1.
    Z74800 Genomic DNA. Translation: CAA99067.1.
    X07070 Genomic DNA. Translation: CAA30106.1.
    BK006948 Genomic DNA. Translation: DAA10725.2.
    PIRiS59291. AJBYRS.
    RefSeqiNP_014583.2. NM_001183313.2.

    Genome annotation databases

    EnsemblFungiiYOL058W; YOL058W; YOL058W.
    GeneIDi854096.
    KEGGisce:YOL058W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35237 Genomic DNA. Translation: AAA34437.1 .
    X91067 Genomic DNA. Translation: CAA62528.1 .
    Z74800 Genomic DNA. Translation: CAA99067.1 .
    X07070 Genomic DNA. Translation: CAA30106.1 .
    BK006948 Genomic DNA. Translation: DAA10725.2 .
    PIRi S59291. AJBYRS.
    RefSeqi NP_014583.2. NM_001183313.2.

    3D structure databases

    ProteinModelPortali P22768.
    SMRi P22768. Positions 3-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34343. 17 interactions.
    DIPi DIP-1660N.
    IntActi P22768. 4 interactions.
    MINTi MINT-393127.
    STRINGi 4932.YOL058W.

    Proteomic databases

    MaxQBi P22768.
    PaxDbi P22768.
    PeptideAtlasi P22768.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL058W ; YOL058W ; YOL058W .
    GeneIDi 854096.
    KEGGi sce:YOL058W.

    Organism-specific databases

    CYGDi YOL058w.
    SGDi S000005419. ARG1.

    Phylogenomic databases

    eggNOGi COG0137.
    GeneTreei ENSGT00390000004524.
    HOGENOMi HOG000230093.
    KOi K01940.
    OMAi PECEYIR.
    OrthoDBi EOG7KSXJR.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00113 .
    BioCyci YEAST:YOL058W-MONOMER.

    Miscellaneous databases

    NextBioi 975761.
    PROi P22768.

    Gene expression databases

    Genevestigatori P22768.

    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. "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].
    2. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
      Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
      Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 90843 / S288c / FY73.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 329-332.
      Strain: ATCC 204508 / S288c.
    5. "Arginine repression of the Saccharomyces cerevisiae ARG1 gene. Comparison of the ARG1 and ARG3 control regions."
      Crabeel M., Seneca S., Devos K., Glansdorff N.
      Curr. Genet. 13:113-124(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
    6. "Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes."
      Jauniaux J.-C., Urrestarazu L.A., Wiame J.-M.
      J. Bacteriol. 133:1096-1107(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Yeast argininosuccinate synthetase. Purification; structural and kinetic properties."
      Hilger F., Simon J.-P., Stalon V.
      Eur. J. Biochem. 94:153-163(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiASSY_YEAST
    AccessioniPrimary (citable) accession number: P22768
    Secondary accession number(s): D6W209
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1870 molecules/cell in log phase SD medium.1 Publication

    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
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3