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D2P5F7 (D2P5F7_LISM2) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginine biosynthesis bifunctional protein ArgJ HAMAP-Rule MF_01106
Gene names
Name:argJ HAMAP-Rule MF_01106
Ordered Locus Names:LM5923_1689
OrganismListeria monocytogenes serotype 1/2a (strain 08-5923) [Complete proteome] [HAMAP] EMBL ADB71530.1
Taxonomic identifier637381 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria ›

Protein attributes

Sequence length398 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 site1851Nucleophile By similarity HAMAP-Rule MF_01106
Binding site1481Substrate By similarity HAMAP-Rule MF_01106
Binding site1741Substrate By similarity HAMAP-Rule MF_01106
Binding site1851Substrate By similarity HAMAP-Rule MF_01106
Binding site2711Substrate By similarity HAMAP-Rule MF_01106
Binding site3931Substrate By similarity HAMAP-Rule MF_01106
Binding site3981Substrate 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
Site1141Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site184 – 1852Cleavage; by autolysis By similarity HAMAP-Rule MF_01106

Sequences

Sequence LengthMass (Da)Tools
D2P5F7 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 04DCBEC67CC2C571

FASTA39842,766
        10         20         30         40         50         60 
MELIKGNIAS PKGFYADGKH AGLKRKRNDI GWIYSEVPAN AAAVYTMNQM QAAPIFVTKD 

        70         80         90        100        110        120 
SFQSNAKLQA IIVNSGNANA CTGNQGMLDA LAMRAQTAEK LEIPLDSVAV ASTGIIGDML 

       130        140        150        160        170        180 
PMDKIITGIE MLEKQTGNAA DFEEAILTTD TFQKQISFQT EIGGRKVTMS GVAKGSGMIH 

       190        200        210        220        230        240 
PNMATMLAFI TTDAAIPAEL LQKLLKIKVD KTFNQITVDG DTSTNDMVVV MANGCAENPM 

       250        260        270        280        290        300 
LQEGTADFAK FADMFQAVTE HLAKSIARDG EGATKLIEVQ VNGATKTEDA RMIAKKIVSS 

       310        320        330        340        350        360 
SLVKTAAFGG DGNWGRIICA IGYSGGRFAP DNITIKIGGI EILNHSSQTI YNQQALDAYL 

       370        380        390 
EEEHIIIEVD LHIGLESGTA WGCDLSYEYV KINACYRT

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References

[1]"High-throughput genome sequencing of two Listeria monocytogenes clinical isolates during a large foodborne outbreak."
Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H., Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.
BMC Genomics 11:120-120(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 08-5923 EMBL ADB71530.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001604 Genomic DNA. Translation: ADB71530.1.
RefSeqYP_003416892.1. NC_013768.1.

3D structure databases

ProteinModelPortalD2P5F7.
SMRD2P5F7. Positions 1-396.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB71530; ADB71530; LM5923_1689.
GeneID8758483.
KEGGlmy:LM5923_1689.
PATRIC32257150. VBILisMon5116_1704.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000022797.
KOK00620.
OMAPNMGTML.

Enzyme and pathway databases

BioCycLMON637381:GH7Z-1685-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. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD2P5F7_LISM2
AccessionPrimary (citable) accession number: D2P5F7
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: May 1, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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