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Q8YPF9 (ARGJ2_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. 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 2

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=AGSase
Gene names
Name:argJ2
Ordered Locus Names:alr4235
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length387 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 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

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

Acetyl-CoA + L-glutamate = CoA + 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.

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. HAMAP-Rule MF_01106

Sequence similarities

Belongs to the ArgJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002099
Chain180 – 387208Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002100

Sites

Active site1801Nucleophile By similarity
Binding site1471Substrate By similarity
Binding site1691Substrate By similarity
Binding site1801Substrate By similarity
Binding site2591Substrate By similarity
Binding site3821Substrate By similarity
Binding site3871Substrate By similarity
Site1101Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity
Site1111Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity
Site179 – 1802Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YPF9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B4A340DC3FF3013D

FASTA38741,146
        10         20         30         40         50         60 
MSLTASSTPQ GFSTFITNLG IRDTTEDFVF LRSDVPCVAD GVFTQSLFAG PSVTISRQNL 

        70         80         90        100        110        120 
QDGQAQGIII ISKNANVANG AVGIADAQEI IQLVAQETGI AAENLAIAST GVIGRRYPIE 

       130        140        150        160        170        180 
KIRAGLVGMG QKLTAADFDL AARGIMTTDT VSKIAARQVG NAKLVGIAKG VGMIEPNMAT 

       190        200        210        220        230        240 
MLAFFFTDAA ISANTLRQIF RSTIDKTFNC LSIDTDTSTS DSAVILANGL AGEVPEAEFA 

       250        260        270        280        290        300 
SALQEIAHDL VLKIARDGEG ATKVIEVTVD SAANYAQAKR VAKAIVNSPL VKTAVYGADP 

       310        320        330        340        350        360 
NWGRVAMAIG KCEDERDINP DQVVIRFDEV QVYPNTFQAE NLEKLKEIMS KEKVNIHVSL 

       370        380 
NIGTDVATVW GCDLTEGYVE INGKYST 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB75934.1.
PIRAD2335.
RefSeqNP_488275.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YPF9.
SMRQ8YPF9. Positions 8-383.
ModBaseSearch...

Protein-protein interaction databases

STRING103690.alr4235.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB75934; BAB75934; BAB75934.
GeneID1107837.
KEGGana:alr4235.
PATRIC22779027. VBINosSp37423_4961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHOG000022797.
KOK00620.
OMAIEENAYY.
ProtClustDBPRK05388.

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 nameARGJ2_NOSS1
AccessionPrimary (citable) accession number: Q8YPF9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 72 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