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Reviewed, UniProtKB/Swiss-Prot P63573 (ARGJ_NEIMA)

Last modified November 3, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginine biosynthesis bifunctional protein argJ
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine biosynthesis bifunctional protein argJ alpha chain
    2- Recommended name:
            Arginine biosynthesis bifunctional protein argJ beta chain
Including the following 2 domains:
    1- Recommended name:
            Glutamate N-acetyltransferase
              EC=2.3.1.35
        Alternative name(s):
            Ornithine acetyltransferase
              Short name=OATase
            Ornithine transacetylase
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS
Gene names
Name: argJ
Ordered Locus Names: NMA0435
OrganismNeisseria meningitidis serogroup A [Complete proteome] [HAMAP]
Taxonomic identifier65699 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

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.

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.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Arginine biosynthesis bifunctional protein argJ alpha chain By similarity
PRO_0000002199
Chain190 – 406217Arginine biosynthesis bifunctional protein argJ beta chain By similarity
PRO_0000002200

Sites

Site189 – 1902Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P63573-1 [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

AL157959 Genomic DNA. Translation: CAM07722.1.
RefSeqYP_002341933.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID906436.
GenomeReviewsGene locus NMA0435 in contig AL157959_GR.
KEGGnma:NMA0435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP63573.
OMAIVNSGNA.

Enzyme and pathway databases

BioCycNMEN122587:NMA0435-MON.
BRENDA2.3.1.1. 292829.
2.3.1.35. 292829.

Family and domain databases

HAMAPMF_01106.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
[Graphical view]
PANTHERPTHR23100. ArgJ. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. ArgJ. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_NEIMA
AccessionPrimary (citable) accession number: P63573
Secondary accession number(s): A1IPQ1, Q9JRJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 3, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents