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

FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine (By similarity).
CATALYTIC ACTIVITY: Succinyl-CoA + L-arginine = CoA + N²-succinyl-L-arginine.
PATHWAY: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5 .
SIMILARITY: Belongs to the arginine N-succinyltransferase 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

AE005674; AAN43072.2; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP16965.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_707365.2; -.
NP_837158.1; -.

3D structure databases

ModBase

Q83L52.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN43072.1-MON; -.

Ontologies

GO:0008791;	Molecular function: arginine N-succinyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0019544;	Biological process: arginine catabolic process to glutamate (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01171; -; 1.
PBIL [Tree]

InterPro

IPR007041; Arg_N-succinyl-Trfase_bsu.
IPR017650; Arginine_N-succinyltransferase.
Graphical view of domain structure.

Pfam

PF04958; AstA; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR03243; arg_catab_AOST; 1.

ProtoNet

Q83L52.

Genome annotation databases

GeneID

1024657; -.
1077968; -.

GenomeReviews

AE014073_GR; S1596.
AE005674_GR; SF1479.

KEGG

sfl:SF1479; -.
sfx:S1596; -.

Phylogenomic databases

HOGENOM

Q83L52; -.

Genome annotation databases

CMR

Q83L52; SF1479.

Other

UniRef

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

Keywords

Acyltransferase; Arginine metabolism; Complete proteome; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 344`	`344`	`Arginine N-succinyltransferase.`	`PRO_0000262332`
`ACT_SITE`	`229 229`		`Proton donor (Potential).`
`BINDING`	`125 125`		`Succinyl-CoA; via amide nitrogen (Potential).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 38428 Da [This is the MW of the unprocessed precursor]

CRC64: 0B4D80412A880BF1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMVIRPVERS DVSALMQLAS KTGGGLTSLP ANEATLSARI ERAIKTWQGE LPKSEQGYVF 

        70         80         90        100        110        120 
VLEDSETGTV AGICAIEVAV GLNDPWYNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS 

       130        140        150        160        170        180 
ELCTLFLDPD WRKEGNGYLL SKSRFMFMAA FRDKFNDKVV AEMRGVIDEH GYSPFWQSLG 

       190        200        210        220        230        240 
KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSQE AQDVIGQVHP QTAPARAVLE 

       250        260        270        280        290        300 
KEGFRYRNYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAQGDFPAC LVANENYHHF 

       310        320        330        340 
RVVLARTDPA TERLILTAAQ LDALKCHAGD RVRLVRLCAE EKTA

Q83L52 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