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B7HNP8 (B7HNP8_BACC7) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. 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 ACJ80268.1
Ordered Locus Names:BCAH187_A4265 EMBL ACJ80268.1
OrganismBacillus cereus (strain AH187) [Complete proteome] [HAMAP] EMBL ACJ80268.1
Taxonomic identifier405534 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length407 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 site1941Nucleophile By similarity HAMAP-Rule MF_01106
Binding site1571Substrate By similarity HAMAP-Rule MF_01106
Binding site1831Substrate By similarity HAMAP-Rule MF_01106
Binding site1941Substrate By similarity HAMAP-Rule MF_01106
Binding site2801Substrate By similarity HAMAP-Rule MF_01106
Binding site4021Substrate By similarity HAMAP-Rule MF_01106
Binding site4071Substrate By similarity HAMAP-Rule MF_01106
Site1201Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site1211Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site193 – 1942Cleavage; by autolysis By similarity HAMAP-Rule MF_01106

Sequences

Sequence LengthMass (Da)Tools
B7HNP8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 73027304CDFF399D

FASTA40744,007
        10         20         30         40         50         60 
MIKVASITKV ENGSIVTPKG FSAIGNAIGL KKEKKDLGAI ICDIPASCAA VYTTNQIQAA 

        70         80         90        100        110        120 
PLQVTKDSIT TEGKLQAIIV NSGNANACTG MKGLQDAYEM RALGAKHFGM KDNYVAVAST 

       130        140        150        160        170        180 
GVIGVPLPMD IIRNGIATLI PAKEEREAHS FSEAILTTDL ITKETCYEMV IDGKKVLIAG 

       190        200        210        220        230        240 
VAKGSGMIHP NMATMLSFIT TDAHIEHDVL QTALSQITNH TFNQITVDGD TSTNDMVIVM 

       250        260        270        280        290        300 
ASGLSETKPI DMEHADWETF IFALQKVCED LAKKIAQDGE GATKLIEVNV LGARTNEEAK 

       310        320        330        340        350        360 
KIAKQIVGSS LVKTAIHGED PNWGRIISSI GQSEVTINPN TIDITLQSIA VLKNSEPQMF 

       370        380        390        400 
SEEEMKMRLQ EHEIMIDVYL HLGEETGSAW GCDLSYEYVK INACYRT

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References

[1]"Genome sequence of Bacillus cereus AH187."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AH187 EMBL ACJ80268.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001177 Genomic DNA. Translation: ACJ80268.1.
RefSeqYP_002340195.1. NC_011658.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING405534.BCAH187_A4265.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ80268; ACJ80268; BCAH187_A4265.
GeneID7077167.
KEGGbcr:BCAH187_A4265.
PATRIC18833955. VBIBacCer120511_4448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHOG000022797.
KOK00620.
OMAPNMGTML.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBCER405534:GHXM-3100-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 nameB7HNP8_BACC7
AccessionPrimary (citable) accession number: B7HNP8
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info