NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
ENZYME REGULATION: Feedback inhibition by L-arginine (By similarity).
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4 .
SUBUNIT: Homohexamer (Probable).
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
SIMILARITY: Contains 1 N-acetyltransferase domain.

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

AE005674; AAN44316.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP18141.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_708609.2; -.
NP_838331.1; -.

3D structure databases

ModBase

P59293.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN44316.1-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:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01105; -; 1.
PBIL [Tree]

InterPro

IPR016181; Acyl_CoA_acyltransferase.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR000182; GCN5-rel_AcTrfase.
IPR010167; NH2A_AcTrfase_ArgA.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.
G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.

Pfam

PF00696; AA_kinase; 1.
PF00583; Acetyltransf_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000423; ArgA; 1.

TIGRFAMs

TIGR01890; N-Ac-Glu-synth; 1.

PROSITE

PS51186; GNAT; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P59293.

Genome annotation databases

GeneID

1025049; -.
1079294; -.

GenomeReviews

AE014073_GR; S3026.
AE005674_GR; SF2829.

KEGG

sfl:SF2829; -.
sfx:S3026; -.

Phylogenomic databases

HOGENOM

P59293; -.

Genome annotation databases

CMR

P59293; SF2829.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 443`	`443`	`Amino-acid acetyltransferase.`	`PRO_0000186807`
`DOMAIN`	`296 443`	`148`	`N-acetyltransferase.`

Sequence information

Length: 443 AA [This is the length of the unprocessed precursor]

Molecular weight: 49209 Da [This is the MW of the unprocessed precursor]

CRC64: 6A3C3EDF90170B47 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKERKTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHE NFSSIVNDIG LLHSLGIRLV 

        70         80         90        100        110        120 
VVYGARPQID ANLAAHHHEP LYHKNIRVTD AKTLELVKQA AGTLQLDITA RLSMSLNNTP 

       130        140        150        160        170        180 
LQGAHINVVS GNFIIAQPLG VDDGVDYCHS GRIRRIDEDA LHRQLESGAI VLMGPVAVSV 

       190        200        210        220        230        240 
TGESFNLTSE EIATQLAIKL KAEKMIGFCS SQGVTNDDGD IVSELFPNEA QARVEAQEEK 

       250        260        270        280        290        300 
GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGALLQEL FSRDGIGTQI VMESAEQIRR 

       310        320        330        340        350        360 
ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNTTIACA ALYPFPEEKI 

       370        380        390        400        410        420 
GEMACVAVHP DYRSSSRGEV LLERIAAQAK QSGLSKLFVL TTRSIHWFQE RGFTPVDIDL 

       430        440 
LPESKKQLYN YQRKSKVLMA DLG

P59293 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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