Skip Header

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

P63574 (ARGJ_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:NMB2005
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length406 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 – 189189Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002201
Chain190 – 406217Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002202

Sites

Site189 – 1902Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P63574 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 0915D50CE69CA656

FASTA40642,812
        10         20         30         40         50         60 
MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP 

        70         80         90        100        110        120 
VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVLPFSTG 

       130        140        150        160        170        180 
VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDKH TVRATGIAKG 

       190        200        210        220        230        240 
SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK 

       250        260        270        280        290        300 
NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTRDEARQAA 

       310        320        330        340        350        360 
YAVARSPLVK TAFFASDPNL GRLLAAIGYA GVADLDTDLV EMYLDDILVA EHGGRAASYT 

       370        380        390        400 
EAQGQAVMSK AEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002098 Genomic DNA. Translation: AAF42332.1.
PIRC81017.
RefSeqNP_274997.1. NC_003112.2.

3D structure databases

ProteinModelPortalP63574.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000010441; EBNEIP00000010061; EBNEIG00000010441.
GeneID904115.
GenomeReviewsGene locus NMB2005 in contig AE002098_GR.
KEGGnme:NMB2005.
PATRIC20360109. VBINeiMen85645_2559.
TIGRNMB2005.

Phylogenomic databases

GeneTreeEBGT00050000020225.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycNMEN122586:NMB_2005-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_NEIMB
AccessionPrimary (citable) accession number: P63574
Secondary accession number(s): Q9JRJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 53 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