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D2BPS8 (D2BPS8_LACLK) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 33. Feed History...

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

Names and origin

Protein namesRecommended name:
Arginine biosynthesis bifunctional protein ArgJ HAMAP-Rule MF_01106
Gene names
Name:argJ HAMAP-Rule MF_01106 EMBL ADA64553.1
Ordered Locus Names:LLKF_0818 EMBL ADA64553.1
OrganismLactococcus lactis subsp. lactis (strain KF147) [Complete proteome] [HAMAP] EMBL ADA64553.1
Taxonomic identifier684738 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate By similarity. HAMAP-Rule MF_01106

Catalytic activity

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

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

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

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity. HAMAP-Rule MF_01106

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01106.

Miscellaneous

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

Sequence similarities

Belongs to the ArgJ family. HAMAP-Rule MF_01106

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1841Nucleophile By similarity HAMAP-Rule MF_01106
Binding site1471Substrate By similarity HAMAP-Rule MF_01106
Binding site1731Substrate By similarity HAMAP-Rule MF_01106
Binding site1841Substrate By similarity HAMAP-Rule MF_01106
Binding site2701Substrate By similarity HAMAP-Rule MF_01106
Binding site3911Substrate By similarity HAMAP-Rule MF_01106
Binding site3961Substrate By similarity HAMAP-Rule MF_01106
Site1121Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site1131Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site183 – 1842Cleavage; by autolysis By similarity HAMAP-Rule MF_01106

Sequences

Sequence LengthMass (Da)Tools
D2BPS8 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: 51534E125DABCBF7

FASTA39642,130
        10         20         30         40         50         60 
MKEIKGTIAS PKGFLADAVH AQLKYKNLDL GLILSQVPAA IAGVFTTNKV CAAPVLIDRQ 

        70         80         90        100        110        120 
IVKNGQARAI 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 KGAPNDLAAR FIAKKIVGSS 

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

       370        380        390 
DKIEIIADLN AGSGLGQAWG CDLTYKYVEI NALYTS 

« Hide

References

[1]"Genome-scale genotype-phenotype matching of two Lactococcus lactis isolates from plants identifies mechanisms of adaptation to the plant niche."
Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D., van Hylckama Vlieg J.E.
Appl. Environ. Microbiol. 74:424-436(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KF147 EMBL ADA64553.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001834 Genomic DNA. Translation: ADA64553.1.
RefSeqYP_003353274.1. NC_013656.1.

3D structure databases

ProteinModelPortalD2BPS8.
SMRD2BPS8. Positions 184-394.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADA64553; ADA64553; LLKF_0818.
GeneID8678239.
KEGGllk:LLKF_0818.
PATRIC32250113. VBILacLac141273_0830.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000022797.
KOK00620.
OMAINADYRT.
OrthoDBEOG6P8TQQ.

Enzyme and pathway databases

BioCycLLAC684738:GI3F-858-MONOMER.
UniPathwayUPA00068; UER00106.
UPA00068; UER00111.

Family and domain databases

Gene3D3.60.70.12. 1 hit.
HAMAPMF_01106. ArgJ.
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. ArgJ-like_dom.
[Graphical view]
PANTHERPTHR23100. PTHR23100. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. Arg_biosynth_ArgJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56266. SSF56266. 1 hit.
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD2BPS8_LACLK
AccessionPrimary (citable) accession number: D2BPS8
Entry history
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)