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Entry version 95 (05 Jun 2019)
Sequence version 2 (09 Jan 2013)
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Protein

Arginine biosynthesis bifunctional protein ArgJ, mitochondrial

Gene

ADR138C

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
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>
-Protein inferred from homologyi <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 annotation

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 <a href="http://www.uniprot.org/help/function_section">'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
Proteins known to be involved in this subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (ADR138C)
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 (ADR138C)
  2. ADL062Wp (AGOS_ADL062W)
  3. ADL062Wp (AGOS_ADL062W)
  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)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>Sitei137Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation1
Sitei138Involved 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_section">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 sitei179SubstrateUniRule annotation1
Binding sitei206SubstrateUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei217NucleophileUniRule annotation1
Binding sitei217SubstrateUniRule annotation1
Binding sitei303SubstrateUniRule annotation1
Binding sitei438SubstrateUniRule annotation1
Binding sitei443SubstrateUniRule 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

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
T05.001

<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_and_taxonomy_section">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, mitochondrialUniRule 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_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:ADR138C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri284811 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000591 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003980101 – 216Arginine biosynthesis bifunctional protein ArgJ alpha chainUniRule annotationAdd BLAST216
ChainiPRO_0000398011217 – 443Arginine biosynthesis bifunctional protein ArgJ beta chainUniRule annotationAdd BLAST227

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei216 – 217Cleavage; 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_section">'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_section">'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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
33169.AAS52058

<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

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SMRi
Q759Y5

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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000022798

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q759Y5

KEGG Orthology (KO)

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KOi
K00620

Identification of Orthologs from Complete Genome Data

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OMAi
GMIAPNM

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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q759Y5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKSSLSLCQR AANAASKYER YVPSCGVFPL GFKVGSIATG VKKNGQLDLG
60 70 80 90 100
VILSTYEREG GATAAAVFTT NKFKAAPVVA SKERLAKSEG RGISAIVVNS
110 120 130 140 150
GCANAVTGAV GLENANKVVQ LVEQQLGRKD TTLLMSTGVI GQHLSMDKIE
160 170 180 190 200
HGLGTLLNND DAFGNDFSSW LSLSKAMMTT DTFPKLISSR FTLPGGTTYT
210 220 230 240 250
LTGISKGAGM ICPNMATLLG FIGTDLPISP SALQNILSSA VDRSFNCISV
260 270 280 290 300
DGDMSTNDTI YMLASGAIDT DLITESSESF PLIKAQVTEL AQNLAQLVVR
310 320 330 340 350
DGEGSTKFVT VHVKRALNFA DAKVIAKTIS NSSLVKCALY GQDANWGRIL
360 370 380 390 400
CAIGYAQLGD CASLDESTLN VSFVGVGDSK GAELNLVVDG VPNVNINESK
410 420 430 440
AATMLADTDL KIVVDLGTGT EECNFWTCDL SHEYISINAD YRS
Length:443
Mass (Da):46,684
Last modified:January 9, 2013 - v2
<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:iD4C1FD97806B9C64
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE016817 Genomic DNA Translation: AAS52058.2

NCBI Reference Sequences

More...
RefSeqi
NP_984234.2, NM_209587.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
AAS52058; AAS52058; AGOS_ADR138C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4620395

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ago:AGOS_ADR138C

<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
AE016817 Genomic DNA Translation: AAS52058.2
RefSeqiNP_984234.2, NM_209587.2

3D structure databases

SMRiQ759Y5
ModBaseiSearch...

Protein-protein interaction databases

STRINGi33169.AAS52058

Protein family/group databases

MEROPSiT05.001

Genome annotation databases

EnsemblFungiiAAS52058; AAS52058; AGOS_ADR138C
GeneIDi4620395
KEGGiago:AGOS_ADR138C

Phylogenomic databases

HOGENOMiHOG000022798
InParanoidiQ759Y5
KOiK00620
OMAiGMIAPNM

Enzyme and pathway databases

UniPathwayiUPA00068;UER00106
UPA00068;UER00111

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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_ASHGO
<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: Q759Y5
<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_and_isoforms">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: January 9, 2013
Last modified: June 5, 2019
This is version 95 of the entry and version 2 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 programFungal 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

Complete proteome, Reference proteome

Documents

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