[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.; Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate (By similarity).
CATALYTIC ACTIVITY: N-succinyl-L-glutamate + H₂O = succinate + L-glutamate.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5 .
SIMILARITY: Belongs to the aspA/astE family. Succinylglutamate desuccinylase subfamily.

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

CP000886; ABX67423.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001588256.1; -.

3D structure databases

ModBase

A9N274.

Ontologies

GO:0016788;	Molecular function: hydrolase activity, acting on ester bonds (inferred from electronic annotation from HAMAP).
GO:0009017;	Molecular function: succinylglutamate desuccinylase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019544;	Biological process: arginine catabolic process to glutamate (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00767; -; 1.
PBIL [Tree]

InterPro

IPR016681; SuccinylGlu_desuccinylase.
Graphical view of domain structure.

PIRSF

PIRSF017020; AstE; 1.

TIGRFAMs

TIGR03242; arg_catab_astE; 1.

ProtoNet

A9N274.

Genome annotation databases

GeneID

5780528; -.

GenomeReviews

CP000886_GR; SPAB_02036.

KEGG

spq:SPAB_02036; -.

CMR

A9N274; SPAB_02036.

Other

UniRef

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

Keywords

Arginine metabolism; Complete proteome; Hydrolase; Metal-binding; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 322`	`322`	`Succinylglutamate desuccinylase.`	`PRO_1000083547`
`ACT_SITE`	`210 210`		`Potential.`
`METAL`	`53 53`		`Zinc (By similarity).`
`METAL`	`56 56`		`Zinc (By similarity).`
`METAL`	`147 147`		`Zinc (By similarity).`

Sequence information

Length: 322 AA [This is the length of the unprocessed precursor]

Molecular weight: 35549 Da [This is the MW of the unprocessed precursor]

CRC64: A4FAFDF92D1A47DF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDNFLALTLS GTTPRVTQGK GAGFRWRWLG HGLLELTPDA PVDRALILSA GIHGNETAPV 

        70         80         90        100        110        120 
EMLDRLLSAL FSGSLTLTWR VLVVLGNPQA LAAGIRYCHS DMNRMFGGRW QSFAESDETR 

       130        140        150        160        170        180 
RARELELSLE TFFSSGQARV RWHLDLHTAI RGSHHLRFGV LPQRDRPWET DFLAWLGAAG 

       190        200        210        220        230        240 
LEALVFHQAP GGTFTHFSSE HFGALSCTLE LGKALPFGQN DLTQFNVTSQ ALSALLSGVE 

       250        260        270        280        290        300 
TSTSSSPPLR YRVVSQITRH SDKFALYMDV QTLNFTVFAK GTLLAEEGDK RVTVTHDVEY 

       310        320 
VLFPNPSVAC GLRAGLMLER LP

A9N274 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