Q8YPF9 (ARGJ2_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine biosynthesis bifunctional protein ArgJ 2

Cleaved into the following 2 chains:

1. Arginine biosynthesis bifunctional protein ArgJ2 alpha chain
2. Arginine biosynthesis bifunctional protein ArgJ2 beta chain

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:	argJ2
Ordered Locus Names:	alr4235

Organism

Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Autocatalytic cleavage
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 179	179	Arginine biosynthesis bifunctional protein ArgJ2 alpha chain By similarity		PRO_0000002099
	Chain	180 – 387	208	Arginine biosynthesis bifunctional protein ArgJ2 beta chain By similarity		PRO_0000002100
Sites
	Site	179 – 180	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YPF9 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: B4A340DC3FF3013D	FASTA	387	41,146
	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

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. , 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: BAB75934.1.
PIR	AD2335.
RefSeq	NP_488275.1. NC_003272.1.
3D structure databases
ProteinModelPortal	Q8YPF9.
SMR	Q8YPF9. Positions 8-383.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8YPF9.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1107837.
GenomeReviews	Gene locus alr4235 in contig BA000019_GR.
KEGG	ana:alr4235.
NMPDR	fig|103690.1.peg.4542.
PATRIC	22779027. VBINosSp37423_4961.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	PTFNSVT.
PhylomeDB	Q8YPF9.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	NSP103690:ALR4235-MONOMER.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
KO	K00620.
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. Arg_biosynth_ArgJ. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ2_NOSS1

Accession

Primary (citable) accession number: Q8YPF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program