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Q486G0 (ARGJ_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginine biosynthesis bifunctional protein ArgJ

Including the following 2 domains:

  1. Glutamate N-acetyltransferase
    EC=2.3.1.35
    Alternative name(s):
    Ornithine acetyltransferase
    Short name=OATase
    Ornithine transacetylase
  2. Amino-acid acetyltransferase
    EC=2.3.1.1
    Alternative name(s):
    N-acetylglutamate synthase
    Short name=AGS
Gene names
Name:argJ
Ordered Locus Names:CPS_1312
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

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

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

Subunit structure

Heterotetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm Probable HAMAP MF_01106.

Miscellaneous

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

Sequence similarities

Belongs to the ArgJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000227218
Chain203 – 424222Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000227219

Sites

Site202 – 2032Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q486G0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 7CB77CFF3C2C81F2

FASTA42444,899
        10         20         30         40         50         60 
MPVNLPEIVP ASLTPIQGIR LGWAESNIKT QNRKDLLVIE ICDGSAVSGV FTQNRFCAAP 

        70         80         90        100        110        120 
VTLCKKHLDA VKNNATTGGN VSGIKALVVN TGNANAGTGE QGMLDALTTC QHLAEIMAIP 

       130        140        150        160        170        180 
VESILPFSTG VILEHLPMDK LLAGLPLAVT NLTTDNWADA ASAIMTTDIA PKAYATQVKV 

       190        200        210        220        230        240 
GGESINITGI SKGAGMIHPN MATMLGYVAT DANITQSLLD SMTKEIADLS FNCISVDGDT 

       250        260        270        280        290        300 
STNDSFIVIA TGKSNAVAIT SPNDKGYQEV FDALLETSQY LAKAIVRDGE GATKFITVTV 

       310        320        330        340        350        360 
KGALSIDEAK TIGFSIGKSP LVKTAMFASD PNLGRVLAAI GYASRECDSL ADLDTNQLEL 

       370        380        390        400        410        420 
YFGGLLVAEK GGRAASYKED EGQAIMNEAE IDITVQLHRG NEESTIWTCD FSYDYVKINA 


EYRT 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ27308.1.
RefSeqYP_268055.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ486G0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ486G0.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3521564.
GenomeReviewsGene locus CPS_1312 in contig CP000083_GR.
KEGGcps:CPS_1312.
NMPDRfig|167879.3.peg.1273.
PATRIC21465853. VBIColPsy94388_1178.
TIGRCPS_1312.

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHBG284202.
OMAGRDPNWG.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycCPSY167879:CPS_1312-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]
KOK00620.
PANTHERPTHR23100. ArgJ. 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 nameARGJ_COLP3
AccessionPrimary (citable) accession number: Q486G0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families