Reviewed, UniProtKB/Swiss-Prot O29118 (ARGJ_ARCFU)

Names and origin

Protein names

Recommended name:
    Arginine biosynthesis bifunctional protein argJ
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine biosynthesis bifunctional protein argJ alpha chain
    2- Recommended name:
            Arginine biosynthesis bifunctional protein argJ beta chain
Including the following 2 domains:
    1- Recommended name:
            Glutamate N-acetyltransferase
              EC=2.3.1.35
        Alternative name(s):
            Ornithine acetyltransferase
              Short name=OATase
            Ornithine transacetylase
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS

Gene names

Name:	argJ
Ordered Locus Names:	AF_1147

Organism

Archaeoglobus fulgidus [Complete proteome] [HAMAP]

Taxonomic identifier

2234 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	379 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. HAMAP MF_01106
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
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 170	170	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002269
	Chain	171 – 379	209	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002270
Sites
	Site	170 – 171	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O29118-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 6C568AF50135361B	FASTA	379	41,237
	10 20 30 40 50 60 MEITDIGGVL CNGIKEGKYG LGLVRVRGSI AGVFTQNKIR AAPVIVCEEN IRDGVVEGVI 70 80 90 100 110 120 VNSGNANAYT GEQGMRDARE MCRIAANLLG CEERRVAVAS TGVIGRKLDM EWIRKKAPEV 130 140 150 160 170 180 YSGLGNSVEN AERFGRAIVT TDRFVKKAYS EKARIAAVAK GAGMIAPNMA TMLCFAFTSA 190 200 210 220 230 240 KFDSGELYDM LRRAADKTFN RLTVDGDTST NDTVLLISTG KERVERDVFE EELCSVFYSI 250 260 270 280 290 300 AKQMARDGEG ATKVFEVRVD GARNDEDANL IARAVASSLL VKTAIFGCDP NWGRIIAAAG 310 320 330 340 350 360 YSGADVDERI TLSLSDGRDE VFLIDSGRPL GNEERARVLM EKAEELVIRL RLEKGNGKGF 370 AIGCDLTYDY VKLNAEYTT

References

[1]

"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB90096.1.
PIR	B69393.
RefSeq	NP_069976.1.
3D structure databases
SMR	O29118. Positions 6-376, 171-377.
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1484371.
GenomeReviews	Gene locus AF_1147 in contig AE000782_GR.
KEGG	afu:AF1147.
NMPDR	fig|224325.1.peg.1135.
TIGR	AF_1147.
Phylogenomic databases
HOGENOM	HBG284202.
OMA	QNRFCAA.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_1147-MONOMER.
BRENDA	2.3.1.1. 7576. 2.3.1.35. 7576.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_ARCFU

Accession

Primary (citable) accession number: O29118

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)