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Q8YVA8 (ARGJ1_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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 1

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:argJ1
Ordered Locus Names:alr2073
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length413 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 – 190190Arginine biosynthesis bifunctional protein ArgJ1 alpha chain By similarity
PRO_0000002097
Chain191 – 413223Arginine biosynthesis bifunctional protein ArgJ1 beta chain By similarity
PRO_0000002098

Sites

Site190 – 1912Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YVA8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9268B3EA817D9134

FASTA41342,998
        10         20         30         40         50         60 
MADWQEITGG ITAPKGYRAA GITAGLKPSG LPDLALIVSD VEAIASGVFT TSQVKAACVD 

        70         80         90        100        110        120 
YCRQRLQAKQ SARAILCNAG QANAATGSQG IKDAEESAEL LAKELNISPE LILLASTGVI 

       130        140        150        160        170        180 
GQRIKMDALR NGIPKLIASL TDTGSDAAAG AIITTDLVTK SIALETTIGD RPVRIGGIAK 

       190        200        210        220        230        240 
GSGMIHPNMA TMLAFVTCDA AVSSHLWQQM LTRAADRSFN SITVDGDTST NDSLIALANG 

       250        260        270        280        290        300 
QSRTPAITEV GAESEKLEAM LTAVCQHLAK AIARDGEGAT CLIEVQVTGA HDEQAARQIA 

       310        320        330        340        350        360 
KTIAGSSLVK SAIFGRDPNW GRIAAAAGRA GVPFEQENLQ IQLGDFLLLD NGQPLPFDRA 

       370        380        390        400        410 
AASAYLKQAA TGAYLQQDTV LISVKVGNGH GTGKAWGCDL SYDYVKINAE YTT 

« 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: 11759840] [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: BAB73772.1.
PIRAC2065.
RefSeqNP_486113.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YVA8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YVA8.

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1105668.
GenomeReviewsGene locus alr2073 in contig BA000019_GR.
KEGGana:alr2073.
NMPDRfig|103690.1.peg.2380.
PATRIC22774270. VBINosSp37423_2606.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1364.
HOGENOMHBG284202.
OMAGRDPNWG.
PhylomeDBQ8YVA8.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycNSP103690:ALR2073-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 nameARGJ1_NOSS1
AccessionPrimary (citable) accession number: Q8YVA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 59 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