Glutamate N-acetyltransferase
     (EC 2.3.1.35)
     (Ornithine acetyltransferase)
     (OATase)
     (Ornithine transacetylase)
Amino-acid acetyltransferase
     (EC 2.3.1.1)
     (N-acetylglutamate synthase)
     (AGS)

Contains

Arginine biosynthesis bifunctional protein argJ alpha chain
Arginine biosynthesis bifunctional protein argJ beta chain

Gene name

	Name:	argJ
	OrderedLocusNames:	CT1110

From

Chlorobium tepidum

[TaxID: 1097]

[HAMAP proteome]

Taxonomy

Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49652 / DSM 12025 / TLS;
DOI=10.1073/pnas.132181499; PubMed=12093901 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium.";
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).

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: N²-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate.
CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
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 .
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4 .
SUBUNIT: 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.
SIMILARITY: Belongs to the argJ family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE006470; AAM72343.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_662001.1; -.

3D structure databases

ModBase

P59611.

Protein family/group databases

MEROPS

T05.001; -.

Enzyme and pathway databases

BioCyc

CTEP194439:CT_1110-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004042;	Molecular function: amino-acid N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0004358;	Molecular function: glutamate N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01106; -; 1.
PBIL [Tree]

InterPro

IPR002813; Arg_biosynth_ArgJ.
Graphical view of domain structure.

PANTHER

PTHR23100; ArgJ; 1.

Pfam

PF01960; ArgJ; 1.
Pfam graphical view of domain structure.

ProDom

PD004193; ArgJ; 2.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00120; ArgJ; 1.

ProtoNet

P59611.

Genome annotation databases

1006898; -.

AE006470_GR; CT1110.

cte:CT1110; -.

fig|194439.1.peg.1095; -.

TIGR

CT1110; -.

Phylogenomic databases

HOGENOM

P59611; -.

Other

LinkHub

P59611; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Cytoplasm; Multifunctional enzyme; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`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`
`SITE`	`192 193`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 404 AA [This is the length of the unprocessed precursor]

Molecular weight: 41800 Da [This is the MW of the unprocessed precursor]

CRC64: 5AC194C611AFF6A6 [This is a checksum on the sequence]

        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

P59611 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools