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F8LHH3 (F8LHH3_STREH) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 16. 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 EMBL CCB92793.1
Ordered Locus Names:SALIVB_0487 EMBL CCB92793.1
OrganismStreptococcus salivarius (strain CCHSS3) [Complete proteome] [HAMAP]
Taxonomic identifier1048332 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length397 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 site3921Substrate By similarity HAMAP-Rule MF_01106
Binding site3971Substrate 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
Site183 – 1842Cleavage; by autolysis By similarity HAMAP-Rule MF_01106

Sequences

Sequence LengthMass (Da)Tools
F8LHH3 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: D3CABE81064E6627

FASTA39742,139
        10         20         30         40         50         60 
MKVIDGTIAS PLGFSADGLH AGFKKRKMDF GWIVSEKPAS VAGVYTTNKV IAAPLIVTKT 

        70         80         90        100        110        120 
SVKKAGKMKA IVVNSGVANS CTGTQGLEDA YTMQEWTAEK LGVEPELVGV ASTGIIGELL 

       130        140        150        160        170        180 
PMDTLKNGLS KIVVNGNADD FAKAILTTDT ATKTIAVTET FGRDVVTMAG VAKGSGMIHP 

       190        200        210        220        230        240 
NMATMLGFVT CDANISSDTL QLALSQNVEK TFNQITVDGD TSTNDMVLVM SNGCTLNEEI 

       250        260        270        280        290        300 
LPDTPEFDKF SKMLNFVMQE LAKKIAKDGE GANKLIQVDV VNAPNALDAR MMAKSVVGSS 

       310        320        330        340        350        360 
LVKTAIFGED PNWGRILAAV GYAGVDVPVD NVDIMIGGLP VMLASSPVSF DDEEMKDIMH 

       370        380        390 
DDEVTITVDL HAGHEKGTAW GCDLSYDYVK INALYHT

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References

[1]"Complete genome sequence of the clinical Streptococcus salivarius strain CCHSS3."
Delorme C., Guedon E., Pons N., Cruaud C., Couloux A., Loux V., Chiapello H., Poyart C., Gautier C., Sanchez N., Almeida M., Kennedy S.P., Ehrlich S.D., Gibrat J.F., Wincker P., Renault P.
J. Bacteriol. 193:5041-5042(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCHSS3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FR873481 Genomic DNA. Translation: CCB92793.1.
RefSeqYP_004727320.1. NC_015760.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCB92793; CCB92793; SALIVB_0487.
GeneID10972685.
KEGGssr:SALIVB_0487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00620.

Enzyme and pathway databases

BioCycSSAL1048332:GI6B-494-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 nameF8LHH3_STREH
AccessionPrimary (citable) accession number: F8LHH3
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: May 29, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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