Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9CC14 (ARGJ_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine biosynthesis bifunctional protein ArgJ

Cleaved into the following 2 chains:

  1. Arginine biosynthesis bifunctional protein ArgJ alpha chain
  2. Arginine biosynthesis bifunctional protein ArgJ beta chain

Including the following 2 domains:

  1. Glutamate N-acetyltransferase
    EC=2.3.1.35
    Alternative name(s):
    Ornithine acetyltransferase
    Short name=OATase
    Ornithine transacetylase
  2. Amino-acid acetyltransferase
    EC=2.3.1.1
    Alternative name(s):
    N-acetylglutamate synthase
    Short name=AGS
Gene names
Name:argJ
Ordered Locus Names:ML1407
OrganismMycobacterium leprae [Complete proteome] [HAMAP]
Taxonomic identifier1769 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP MF_01106

Catalytic activity

N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP MF_01106

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm Probable HAMAP MF_01106.

Miscellaneous

Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106

Sequence similarities

Belongs to the ArgJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002189
Chain203 – 407205Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002190

Sites

Site202 – 2032Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CC14 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E5E471A5AC489535

FASTA40741,763
        10         20         30         40         50         60 
MTKIVEIVNE TRLLRAQGVT APAGFQAAGI TAGIKVSGAP DLALVFNEGP DYAAAGVFTR 

        70         80         90        100        110        120 
NKVKAAPVLW TQRVLSTGQL RAVILNSGGA NACTGPAGFQ DAHTTAEAVA AALSDWGTET 

       130        140        150        160        170        180 
GAIEVAVCST GLIGDRLPMD KVLAGVRAIV HKMAGGVTGG DDAAHAIMTT DTVPKQVALH 

       190        200        210        220        230        240 
NRNKWTVGGM AKGAGMLAPS LATMLCVLTT DAVVEPAALD QALRRATAHT FDRLDIDGCC 

       250        260        270        280        290        300 
STNDTVLLLA SGASGITPPQ ADLDDAVRHA CDDLCAQLQA DAEGVTKRVT VTVIGAASDD 

       310        320        330        340        350        360 
DALVAARMIA RDNLVKTAVF GSDPNWGRVL AAVGMAPVAL DPDRLCMSFN GAAVCIDGVG 

       370        380        390        400 
TPCARDVDLS TADIDITVDL RIGDSAATIR TTDLSHTYVE ENSAYSS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL583922 Genomic DNA. Translation: CAC30358.1.
PIRA87085.
RefSeqNP_302000.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ9CC14.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000029122; EBMYCP00000028728; EBMYCG00000029117.
GeneID910546.
GenomeReviewsGene locus ML1407 in contig AL450380_GR.
KEGGmle:ML1407.
NMPDRfig|272631.1.peg.872.
PATRIC18055358. VBIMycLep78757_2612.

Organism-specific databases

LepromaML1407.
CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016724.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycMLEP272631:ML1407-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]
KOK00620.
PANTHERPTHR23100. ArgJ. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. Arg_biosynth_ArgJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_MYCLE
AccessionPrimary (citable) accession number: Q9CC14
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents