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P62062 (ARGJ_LEPIC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LIC_13271
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]
Taxonomic identifier267671 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length385 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 – 178178Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002179
Chain179 – 385207Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002180

Sites

Site178 – 1792Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P62062 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 82F0D90666EF18BE

FASTA38541,503
        10         20         30         40         50         60 
MHMPKGFLSF GINIGIKDDT KDFGVIYSEI PCKATAVFTK NNFPGAPVIV GKEHVRSGVL 

        70         80         90        100        110        120 
QAIVINSKNS NVATGEKGIQ NSREICKIIG ESLDIKETLV LPSSTGVIGV PLKMEIILPA 

       130        140        150        160        170        180 
CKKAKSLLKP GNLEEVAEAI MTTDTRKKIS SRNIKTKSGQ GTIYGIAKGA GMIEPNMATM 

       190        200        210        220        230        240 
LCYILSDVSL PEGTDLYSIL KSSVDQSFNC LTIDSDTSTS DTVALLCNGL SGESSVQDFS 

       250        260        270        280        290        300 
KALTEICIDL TKLIATDGEG ATKLIELTIS GAKSEAQARK IGKSILNSPL VKTAIYGGDP 

       310        320        330        340        350        360 
NWGRLIMAVG KVFDEPIPFE GLQIYFGTLP VKEANPETLK KLSEYLKNNT EISLNVVLNV 

       370        380 
GTISMKFWGC DFTEKYIEEN AYYTT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016823 Genomic DNA. Translation: AAS71815.1.
RefSeqYP_003178.1. NC_005823.1.

3D structure databases

ProteinModelPortalP62062.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2772095.
GenomeReviewsGene locus LIC_13271 in contig AE016823_GR.
KEGGlic:LIC13271.
NMPDRfig|267671.1.peg.3178.
PATRIC22379621. VBILepInt6257_3958.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284202.
OMAPTFNSVT.
PhylomeDBP62062.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycLINT-130-01:LINT-130-01-003178-MONOMER.
LINT267671:LIC_13271-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_LEPIC
AccessionPrimary (citable) accession number: P62062
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: January 25, 2012
This is version 59 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

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