Reviewed, UniProtKB/Swiss-Prot P59611 (ARGJ_CHLTE)

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:	CT1110

Organism

Chlorobium tepidum [Complete proteome] [HAMAP]

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	404 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.
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.
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	amino-acid 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 – 192	192	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002147
	Chain	193 – 404	212	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002148
Sites
	Site	192 – 193	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59611-1 [UniParc]. Last modified April 23, 2003. Version 1. Checksum: 5AC194C611AFF6A6	FASTA	404	41,800
	10 20 30 40 50 60 MRPVVADPAS DAVFWPEGFT LAGINCGIKP TSKDLMLMLC DEPASTASVF TTNLCCAAPV 70 80 90 100 110 120 ELSKAALSAS GGKMRAVICN SGNANAATGA AGMQNARLMA ESTAQAFDLN AGEVLVASTG 130 140 150 160 170 180 VIGQQLPVEK IAGAMPSLKA TSGSTQWCDA AEAIMTTDTF PKAFGVDVKL SGGTARIAGI 190 200 210 220 230 240 AKGSGMICPN MATMLAFLGT DATIEPALLQ ELLAAANAVS FNAITVDGDT STNDMAAIMA 250 260 270 280 290 300 SGKGPEVLRG SDNARLFGEA LRSVMTMLAQ LIIVDGEGAT KFVELRVTGA KSNEEARMAA 310 320 330 340 350 360 MTVANSPLVK TAIHGEDANW GRIIAAAGRS GASFVQEELS VYFDDEPILK PGLDANFSEE 370 380 390 400 RAKEVMSKEE FTITLSLGKG AGRATVWTCD LSHGYIEING SYRS

References

[1]

"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006470 Genomic DNA. Translation: AAM72343.1.
RefSeq	NP_662001.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1006898.
GenomeReviews	Gene locus CT1110 in contig AE006470_GR.
KEGG	cte:CT1110.
NMPDR	fig|194439.1.peg.1095.
TIGR	CT1110.
Phylogenomic databases
HOGENOM	P59611.
OMA	P59611. IVNSGNA.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_1110-MON.
BRENDA	2.3.1.1. 189605. 2.3.1.35. 189605.
Family and domain databases
HAMAP	MF_01106. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. ArgJ. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_CHLTE

Accession

Primary (citable) accession number: P59611

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	April 23, 2003
Last modified:	June 16, 2009
This is version 47 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)