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B7KZ22 (B7KZ22_METC4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 32. 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:Mchl_0358 EMBL ACK81295.1
OrganismMethylobacterium extorquens (strain CM4 / NCIMB 13688) (Methylobacterium chloromethanicum) [Complete proteome] [HAMAP] EMBL ACK81295.1
Taxonomic identifier440085 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium ›

Protein attributes

Sequence length414 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 site1991Nucleophile By similarity HAMAP-Rule MF_01106
Binding site1621Substrate By similarity HAMAP-Rule MF_01106
Binding site1881Substrate By similarity HAMAP-Rule MF_01106
Binding site1991Substrate By similarity HAMAP-Rule MF_01106
Binding site2861Substrate By similarity HAMAP-Rule MF_01106
Binding site4091Substrate By similarity HAMAP-Rule MF_01106
Binding site4141Substrate By similarity HAMAP-Rule MF_01106
Site1231Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site1241Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity HAMAP-Rule MF_01106
Site198 – 1992Cleavage; by autolysis By similarity HAMAP-Rule MF_01106

Sequences

Sequence LengthMass (Da)Tools
B7KZ22 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 9907B6F8EB683E9C

FASTA41442,977
        10         20         30         40         50         60 
MSSTEISPLA PATSPSLPEI AGVRIATAQA GIRYKNRTDV LYVALAEGTQ VAGVFTRSRC 

        70         80         90        100        110        120 
PSAPVDWCRD ALKASKGARA LVVNSGNANA FTGLKGREAV ALTAEIAARV AACAPEAVMI 

       130        140        150        160        170        180 
ASTGVIGEPL DARKFDGVLA ECAGRAEGGA EAWAQAAQAI MTTDTFPKLA TRRVEIDGVP 

       190        200        210        220        230        240 
VTINGIAKGA GMIAPDMATM LSFAFTDAAL PQDVLQDLLS AGTKTSFNCV TVDGDTSTSD 

       250        260        270        280        290        300 
TLLLFATGAA GNAAVTRAED PRLAGFRAAL DDLLIELAQL VARDGEGANK LVTVEVEGAE 

       310        320        330        340        350        360 
SDPSAHRIAM SIANSPLVKT AVAGEDANWG RVVMAVGKAG EPADRDRLAI WFGDVRVAVQ 

       370        380        390        400        410 
GARDPDYSEE AASAVMRRPE ITVRVDLGLG QGRARVWTCD LTKAYVAING DYRS

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium chloromethanicum CM4."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Marx C., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CM4 / NCIMB 13688.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001298 Genomic DNA. Translation: ACK81295.1.
RefSeqYP_002419223.1. NC_011757.1.

3D structure databases

ProteinModelPortalB7KZ22.
ModBaseSearch...

Protein-protein interaction databases

STRING440085.Mchl_0358.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK81295; ACK81295; Mchl_0358.
GeneID7118658.
KEGGmch:Mchl_0358.
PATRIC22494874. VBIMetChl132133_0316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHOG000022798.
KOK00620.
OMAVFTRSKC.
ProtClustDBCLSK2330188.

Enzyme and pathway databases

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 nameB7KZ22_METC4
AccessionPrimary (citable) accession number: B7KZ22
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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