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Reviewed, UniProtKB/Swiss-Prot Q9CHD4 (ARGJ_LACLA)

Last modified November 3, 2009. Version 50. 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: LL0798
ORF Names: L0105
OrganismLactococcus lactis subsp. lactis (Streptococcus lactis) [Complete proteome] [HAMAP]
Taxonomic identifier1360 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length396 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 – 183183Arginine biosynthesis bifunctional protein argJ alpha chain By similarity
PRO_0000002175
Chain184 – 396213Arginine biosynthesis bifunctional protein argJ beta chain By similarity
PRO_0000002176

Sites

Site183 – 1842Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CHD4-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 52C7E72E18B97AA3

FASTA39642,174
        10         20         30         40         50         60 
MKEIKGTIAS PKGFLADAVH AQLKYKNLDL GLILSQVPAA IAGVFTTNKV CAAPVLIDRQ 

        70         80         90        100        110        120 
IVKKGQARAI ICNSAVANAV TGEQGYANAL KTQKLLAEKF ELKAEEVAVC STGVIGVQLP 

       130        140        150        160        170        180 
MEKIATGISK LSQNEGTAAY FAKAILTTDT QTKTINFEAE IGGQIVNMAG VCKGSGMIHP 

       190        200        210        220        230        240 
NMATMLAFIT TDAKIAQALL QKTLSEIIET TFNQITVDGD TSTNDTVLLM ANGQAKNNEI 

       250        260        270        280        290        300 
LEGSSDYLLF KEMLAKVCQS LAKQIAADGE GATKLIEVTV KGAPNDLTAR FIAKKIVGSS 

       310        320        330        340        350        360 
LVKTAIFGAD PNWGRIISSI GQVANFEVSD IELKLQDELV LYHSTPVDFD AAFLSEKLKE 

       370        380        390 
DKIEIIADLN AGSGLGQAWG CDLTYKYVEI NALYTS 

« Hide

References

[1]"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IL1403.

Cross-references

Sequence databases

AE005176 Genomic DNA. Translation: AAK04896.1.
PIRF86724.
RefSeqNP_266954.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Genome annotation databases

GeneID1114425.
GenomeReviewsGene locus LL0798 in contig AE005176_GR.
KEGGlla:L0105.
NMPDRfig|272623.1.peg.818.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9CHD4.
OMAVHENSAY.

Enzyme and pathway databases

BioCycLLAC272623:L0105-MON.
BRENDA2.3.1.1. 278870.
2.3.1.35. 278870.

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_LACLA
AccessionPrimary (citable) accession number: Q9CHD4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2001
Last modified: November 3, 2009
This is version 50 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