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Protein

Arginine biosynthesis bifunctional protein ArgJ, mitochondrial

Gene

ARG7

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 two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.UniRule annotation1 Publication

Catalytic activityi

N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate.UniRule annotation
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.UniRule annotation

Enzyme regulationi

Inhibited by ornithine.1 Publication

Kineticsi

  1. KM=8.4 mM for glutamate1 Publication
  2. KM=2.8 mM for N-acetylornithine1 Publication

    Pathwayi: L-arginine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic).UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (ARG7)
    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-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic), the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

    Pathwayi: L-arginine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Amino-acid acetyltransferase, mitochondrial (ARG2), Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (ARG7)
    2. Protein ARG5,6, mitochondrial (ARG5,6)
    3. Protein ARG5,6, mitochondrial (ARG5,6)
    4. Acetylornithine aminotransferase, mitochondrial (ARG8)
    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 N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei136 – 1361Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation
    Sitei137 – 1371Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation
    Binding sitei177 – 1771SubstrateUniRule annotation
    Binding sitei204 – 2041SubstrateUniRule annotation
    Active sitei215 – 2151NucleophileUniRule annotation
    Binding sitei215 – 2151SubstrateUniRule annotation
    Binding sitei301 – 3011SubstrateUniRule annotation
    Binding sitei436 – 4361SubstrateUniRule annotation
    Binding sitei441 – 4411SubstrateUniRule annotation

    GO - Molecular functioni

    • acetyl-CoA:L-glutamate N-acetyltransferase activity Source: SGD
    • glutamate N-acetyltransferase activity Source: SGD

    GO - Biological processi

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

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis

    Enzyme and pathway databases

    BioCyciYEAST:YMR062C-MONOMER.
    UniPathwayiUPA00068; UER00106.
    UPA00068; UER00111.

    Protein family/group databases

    MEROPSiT05.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine biosynthesis bifunctional protein ArgJ, mitochondrialUniRule annotation
    Alternative name(s):
    Extracellular mutant protein 40
    Cleaved into the following 2 chains:
    Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotation
    Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotation
    Including the following 2 domains:
    Glutamate N-acetyltransferaseUniRule annotation (EC:2.3.1.35UniRule annotation)
    Short name:
    GATUniRule annotation
    Alternative name(s):
    Ornithine acetyltransferaseUniRule annotation
    Short name:
    OATaseUniRule annotation
    Ornithine transacetylaseUniRule annotation
    Amino-acid acetyltransferaseUniRule annotation (EC:2.3.1.1UniRule annotation)
    Alternative name(s):
    N-acetylglutamate synthaseUniRule annotation
    Short name:
    AGSUniRule annotation
    Gene namesi
    Name:ARG7UniRule annotation
    Synonyms:ECM40
    Ordered Locus Names:YMR062C
    ORF Names:YM9916.01C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XIII

    Organism-specific databases

    EuPathDBiFungiDB:YMR062C.
    SGDiS000004666. ARG7.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrial matrix Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi215 – 2151T → A: Blocks autocatalytic processing of the precursor protein. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 88MitochondrionUniRule annotation1 Publication
    Chaini9 – 214206Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotationPRO_0000002283Add
    BLAST
    Chaini215 – 441227Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotationPRO_0000002284Add
    BLAST

    Post-translational modificationi

    The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.UniRule annotation1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei214 – 2152Cleavage; by autolysis

    Keywords - PTMi

    Autocatalytic cleavage

    Proteomic databases

    MaxQBiQ04728.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    BioGridi35237. 52 interactions.
    IntActiQ04728. 1 interaction.
    MINTiMINT-586736.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04728.
    SMRiQ04728. Positions 29-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ArgJ family.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOGENOMiHOG000022798.
    InParanoidiQ04728.
    KOiK00620.
    OMAiWTCDLTH.
    OrthoDBiEOG75J0XC.

    Family and domain databases

    Gene3Di3.60.70.12. 1 hit.
    HAMAPiMF_01106. ArgJ.
    InterProiIPR002813. Arg_biosynth_ArgJ.
    IPR016117. ArgJ-like_dom.
    [Graphical view]
    PANTHERiPTHR23100. PTHR23100. 1 hit.
    PfamiPF01960. ArgJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF56266. SSF56266. 1 hit.
    TIGRFAMsiTIGR00120. ArgJ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q04728-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRISSTLLQR SKQLIDKYAL YVPKTGSFPK GFEVGYTASG VKKNGSLDLG
    60 70 80 90 100
    VILNTNKSRP STAAAVFTTN KFKAAPVLTS KKVLETARGK NINAIVVNSG
    110 120 130 140 150
    CANSVTGDLG MKDAQVMIDL VNDKIGQKNS TLVMSTGVIG QRLQMDKIST
    160 170 180 190 200
    GINKIFGEEK FGSDFNSWLN VAKSICTTDT FPKLVTSRFK LPSGTEYTLT
    210 220 230 240 250
    GMAKGAGMIC PNMATLLGFI VTDLPIESKA LQKMLTFATT RSFNCISVDG
    260 270 280 290 300
    DMSTNDTICM LANGAIDTKE INEDSKDFEQ VKLQVTEFAQ RLAQLVVRDG
    310 320 330 340 350
    EGSTKFVTVN VKNALHFEDA KIIAESISNS MLVKTALYGQ DANWGRILCA
    360 370 380 390 400
    IGYAKLNDLK SLDVNKINVS FIATDNSEPR ELKLVANGVP QLEIDETRAS
    410 420 430 440
    EILALNDLEV SVDLGTGDQA AQFWTCDLSH EYVTINGDYR S
    Length:441
    Mass (Da):47,849
    Last modified:November 1, 1997 - v1
    Checksum:i7AC03B7A72E3CE46
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U90438 Genomic DNA. Translation: AAB49897.1.
    Z48952 Genomic DNA. Translation: CAA88787.1.
    Z49703 Genomic DNA. Translation: CAA89772.1.
    BK006946 Genomic DNA. Translation: DAA09960.1.
    PIRiS52822.
    RefSeqiNP_013778.1. NM_001182560.1.

    Genome annotation databases

    EnsemblFungiiYMR062C; YMR062C; YMR062C.
    GeneIDi855084.
    KEGGisce:YMR062C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U90438 Genomic DNA. Translation: AAB49897.1.
    Z48952 Genomic DNA. Translation: CAA88787.1.
    Z49703 Genomic DNA. Translation: CAA89772.1.
    BK006946 Genomic DNA. Translation: DAA09960.1.
    PIRiS52822.
    RefSeqiNP_013778.1. NM_001182560.1.

    3D structure databases

    ProteinModelPortaliQ04728.
    SMRiQ04728. Positions 29-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35237. 52 interactions.
    IntActiQ04728. 1 interaction.
    MINTiMINT-586736.

    Protein family/group databases

    MEROPSiT05.001.

    Proteomic databases

    MaxQBiQ04728.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYMR062C; YMR062C; YMR062C.
    GeneIDi855084.
    KEGGisce:YMR062C.

    Organism-specific databases

    EuPathDBiFungiDB:YMR062C.
    SGDiS000004666. ARG7.

    Phylogenomic databases

    HOGENOMiHOG000022798.
    InParanoidiQ04728.
    KOiK00620.
    OMAiWTCDLTH.
    OrthoDBiEOG75J0XC.

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00106.
    UPA00068; UER00111.
    BioCyciYEAST:YMR062C-MONOMER.

    Miscellaneous databases

    PROiQ04728.

    Family and domain databases

    Gene3Di3.60.70.12. 1 hit.
    HAMAPiMF_01106. ArgJ.
    InterProiIPR002813. Arg_biosynth_ArgJ.
    IPR016117. ArgJ-like_dom.
    [Graphical view]
    PANTHERiPTHR23100. PTHR23100. 1 hit.
    PfamiPF01960. ArgJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF56266. SSF56266. 1 hit.
    TIGRFAMsiTIGR00120. ArgJ. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Li W., Fitzgerald M.C., Neigeborn L., Mitchell A.P.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SK1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Purification and characterization of ornithine acetyltransferase from Saccharomyces cerevisiae."
      Liu Y., van Heeswijck R., Hoej P., Hoogenraad N.
      Eur. J. Biochem. 228:291-296(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 9-28 AND 215-234, CHARACTERIZATION.
    5. "Characterization of the Saccharomyces cerevisiae ARG7 gene encoding ornithine acetyltransferase, an enzyme also endowed with acetylglutamate synthase activity."
      Crabeel M., Abadjieva A., Hilven P., Desimpelaere J., Soetens O.
      Eur. J. Biochem. 250:232-241(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    6. "The yeast ARG7 gene product is autoproteolyzed to two subunit peptides, yielding active ornithine acetyltransferase."
      Abadjieva A., Hilven P., Pauwels K., Crabeel M.
      J. Biol. Chem. 275:11361-11367(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF THR-215.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. "Continuous spectrophotometric assays for three regulatory enzymes of the arginine biosynthetic pathway."
      Takahara K., Akashi K., Yokota A.
      Anal. Biochem. 368:138-147(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiARGJ_YEAST
    AccessioniPrimary (citable) accession number: Q04728
    Secondary accession number(s): D6VZN6, Q04682, Q09168
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: July 6, 2016
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    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 one 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.