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Protein

Argininosuccinate synthase

Gene

ARG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    Pathway:iL-arginine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Ornithine carbamoyltransferase (ARG3)
    2. Argininosuccinate synthase (ARG1)
    3. Argininosuccinate lyase (ARG4)
    This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

    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

    • argininosuccinate synthase activity Source: SGD
    • ATP binding Source: UniProtKB-KW

    GO - Biological processi

    • arginine biosynthetic process Source: SGD
    Complete GO annotation...

    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.
    ReactomeiREACT_349046. Urea cycle.
    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 Componenti: Chromosome XV

    Organism-specific databases

    CYGDiYOL058w.
    EuPathDBiFungiDB:YOL058W.
    SGDiS000005419. ARG1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

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

    Proteomic databases

    MaxQBiP22768.
    PaxDbiP22768.
    PeptideAtlasiP22768.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

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

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0137.
    GeneTreeiENSGT00390000004524.
    HOGENOMiHOG000230093.
    InParanoidiP22768.
    KOiK01940.
    OMAiIYNGYWW.
    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

    « Hide

            10         20         30         40         50
    MSKGKVCLAY SGGLDTSVIL AWLLDQGYEV VAFMANVGQE EDFDAAKEKA
    60 70 80 90 100
    LKIGACKFVC VDCREDFVKD ILFPAVQVNA VYEDVYLLGT SLARPVIAKA
    110 120 130 140 150
    QIDVAKQEGC FAVSHGCTGK GNDQIRFELS FYALKPDVKC ITPWRMPEFF
    160 170 180 190 200
    ERFAGRKDLL DYAAQKGIPV AQTKAKPWST DENQAHISYE AGILEDPDTT
    210 220 230 240 250
    PPKDMWKLIV DPMDAPDQPQ DLTIDFERGL PVKLTYTDNK TSKEVSVTKP
    260 270 280 290 300
    LDVFLAASNL ARANGVGRID IVEDRYINLK SRGCYEQAPL TVLRKAHVDL
    310 320 330 340 350
    EGLTLDKEVR QLRDSFVTPN YSRLIYNGSY FTPECEYIRS MIQPSQNSVN
    360 370 380 390 400
    GTVRVRLYKG NVIILGRSTK TEKLYDPTES SMDELTGFLP TDTTGFIAIQ
    410 420
    AIRIKKYGES KKTKGEELTL
    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

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

    Proteomic databases

    MaxQBiP22768.
    PaxDbiP22768.
    PeptideAtlasiP22768.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CYGDiYOL058w.
    EuPathDBiFungiDB:YOL058W.
    SGDiS000005419. ARG1.

    Phylogenomic databases

    eggNOGiCOG0137.
    GeneTreeiENSGT00390000004524.
    HOGENOMiHOG000230093.
    InParanoidiP22768.
    KOiK01940.
    OMAiIYNGYWW.
    OrthoDBiEOG7KSXJR.

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00113.
    BioCyciYEAST:YOL058W-MONOMER.
    ReactomeiREACT_349046. Urea cycle.

    Miscellaneous databases

    NextBioi975761.
    PROiP22768.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 134 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.