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Entry version 65 (07 Oct 2020)
Sequence version 1 (22 Nov 2005)
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Protein

Arginine biosynthesis bifunctional protein ArgJ, chloroplastic

Gene
N/A
Organism
Citrullus lanatus (Watermelon) (Citrullus vulgaris)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=3.4 mM for N2-acetyl-L-ornithine (at pH 7.0)
  2. KM=17.8 mM for L-glutamate (at pH 7.0)

    pH dependencei

    Optimum pH is 7.0.

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 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 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)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei163Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation1
    Sitei164Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei202SubstrateUniRule annotation1
    Binding sitei228SubstrateUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei239NucleophileUniRule annotation1
    Binding sitei239SubstrateUniRule annotation1
    Binding sitei328SubstrateUniRule annotation1
    Binding sitei455SubstrateUniRule annotation1
    Binding sitei460SubstrateUniRule annotation1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Multifunctional enzyme, Transferase
    Biological processAmino-acid biosynthesis, Arginine biosynthesis

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q3C251

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00068;UER00106
    UPA00068;UER00111

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    T05.002

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Arginine biosynthesis bifunctional protein ArgJ, chloroplasticUniRule annotation
    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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCitrullus lanatus (Watermelon) (Citrullus vulgaris)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3654 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCitrullus

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Chloroplast, Plastid

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 26ChloroplastUniRule annotation1 PublicationAdd BLAST26
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000039797627 – 238Arginine biosynthesis bifunctional protein ArgJ alpha chainAdd BLAST212
    ChainiPRO_0000397977239 – 460Arginine biosynthesis bifunctional protein ArgJ beta chainAdd BLAST222

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei238 – 239Cleavage; by autolysisUniRule annotation2

    Keywords - PTMi

    Autocatalytic cleavage

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Heterodimer of an alpha and a beta chain.

    UniRule annotation

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q3C251

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the ArgJ family.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02152, OAT, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.20.340, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01106, ArgJ, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002813, Arg_biosynth_ArgJ
    IPR016117, ArgJ-like_dom_sf
    IPR042195, ArgJ_beta_C

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR23100, PTHR23100, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01960, ArgJ, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56266, SSF56266, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00120, ArgJ, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q3C251-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYLSVPHYPS LKFTAFQSHK RNFRVFAVAT NEAANYLPEA PILIPDGPWK
    60 70 80 90 100
    QIDGGVTAAK GFKAAGLYGG LRAKGEKPDL ALVTCDVDAI SAGAFTKNVV
    110 120 130 140 150
    AAAPVLYCKK ALDISETARA VLINAGQANA ATGDAGYQDV IECVNNLSKI
    160 170 180 190 200
    LQIRPEEILV ESTGVIGHRI KKDALLNSLP QLVRSLSSSV GGAASAAVAI
    210 220 230 240 250
    TTTDLVSKSV AIESQVGGST IRIGGMAKGS GMIHPNMATM LGVVTTDAVV
    260 270 280 290 300
    ACDVWRKMVQ ISVDRSFNQI TVDGDTSTND TVIALSSGLS GFNSNIISSL
    310 320 330 340 350
    KSREAGQLQE CLDVVMQGLA KSIAWDGEGA TCLIEITVSG ASTEAEAAKV
    360 370 380 390 400
    ARSVAGSSLV KSAIYGRDPN WGRIAAAAGY AGVPFDQMKL KVSLGNILLM
    410 420 430 440 450
    DGGEPQSFDR AAASNYLRRA GETHDTVRIF ISIGDGQGEG RAWGCDLSYD
    460
    YVKINAEYTT
    Length:460
    Mass (Da):48,203
    Last modified:November 22, 2005 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i50AA2399AC517835
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AB212224 mRNA Translation: BAE46903.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB212224 mRNA Translation: BAE46903.1

    3D structure databases

    SMRiQ3C251
    ModBaseiSearch...

    Protein family/group databases

    MEROPSiT05.002

    Enzyme and pathway databases

    UniPathwayiUPA00068;UER00106
    UPA00068;UER00111
    SABIO-RKiQ3C251

    Family and domain databases

    CDDicd02152, OAT, 1 hit
    Gene3Di3.10.20.340, 1 hit
    HAMAPiMF_01106, ArgJ, 1 hit
    InterProiView protein in InterPro
    IPR002813, Arg_biosynth_ArgJ
    IPR016117, ArgJ-like_dom_sf
    IPR042195, ArgJ_beta_C
    PANTHERiPTHR23100, PTHR23100, 1 hit
    PfamiView protein in Pfam
    PF01960, ArgJ, 1 hit
    SUPFAMiSSF56266, SSF56266, 1 hit
    TIGRFAMsiTIGR00120, ArgJ, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARGJ_CITLA
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q3C251
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: November 22, 2005
    Last modified: October 7, 2020
    This is version 65 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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