Q5PHC2 (ASTE_SALPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinylglutamate desuccinylase
EC=3.5.1.96

Gene names

Name:	astE
Ordered Locus Names:	SPA1537

Organism

Salmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]

Taxonomic identifier

295319 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella paratyphi A

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Transforms N(2)-succinylglutamate into succinate and glutamate By similarity. HAMAP-Rule MF_00767
Catalytic activity	N-succinyl-L-glutamate + H2O = succinate + L-glutamate. HAMAP-Rule MF_00767
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. HAMAP-Rule MF_00767
Sequence similarities	Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.

Ontologies

Keywords
Biological process	Arginine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	arginine catabolic process to glutamate Inferred from electronic annotation. Source: HAMAP arginine catabolic process to succinate Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: HAMAP succinylglutamate desuccinylase activity Inferred from electronic annotation. Source: EC zinc ion binding 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 – 322	322	Succinylglutamate desuccinylase HAMAP-Rule MF_00767		PRO_0000257720
Sites
	Active site	210	1	Potential
	Metal binding	53	1	Zinc By similarity
	Metal binding	56	1	Zinc By similarity
	Metal binding	147	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PHC2 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: E069E4A15EB48AEE	FASTA	322	35,426
	10 20 30 40 50 60 MDNFLALTLS GTTPRVTQGK GAGFRWRWLS HGLLELTPDA PVDRALILSA GIHGNETAPV 70 80 90 100 110 120 EMLDKLLSAL YSGSLTLTWR VLVVLGNPQA LAAGIRYCHS DMNRMFGGRW QSFAESDETR 130 140 150 160 170 180 RARELELSLE TFFSSGQARV RWHLDLHTAI RGSHHLRFGV LPQRDRPWET GFLAWLGAAG 190 200 210 220 230 240 LEALVFHQAP GGTFTHFSSE HFGALSCTLE LGKALPFGQN DLTQFSVTSQ ALSALLSGVE 250 260 270 280 290 300 TSTSSSPPLR YRVVSQITRH SDKFALYMDA QTLNFTAFAK GTLLAEEGDK RVTVTHDVEY 310 320 VLFPNPSVAC GLRAGLMLER LP

References

[1]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000026 Genomic DNA. Translation: AAV77470.1.
RefSeq	YP_150782.1. NC_006511.1.
3D structure databases
HSSP	HSSP built from PDB template 1YW6 based on UniProtKB P76215.
ProteinModelPortal	Q5PHC2.
SMR	Q5PHC2. Positions 1-321.
ModBase	Search...
Protein-protein interaction databases
STRING	295319.SPA1537.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV77470; AAV77470; SPA1537.
GeneID	3174984.
KEGG	spt:SPA1537.
PATRIC	32352418. VBISalEnt134188_1639.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2988.
HOGENOM	HOG000280300.
KO	K05526.
OMA	TAPIEIC.
ProtClustDB	PRK05324.
Enzyme and pathway databases
BioCyc	SENT295319:GJBZ-1537-MONOMER.
UniPathway	UPA00185; UER00283.
Family and domain databases
HAMAP	MF_00767. Arg_catab_AstE.
InterPro	IPR007036. Aste_AspA. IPR016681. SuccinylGlu_desuccinylase. [Graphical view]
Pfam	PF04952. AstE_AspA. 1 hit. [Graphical view]
PIRSF	PIRSF017020. AstE. 1 hit.
TIGRFAMs	TIGR03242. arg_catab_astE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ASTE_SALPA

Accession

Primary (citable) accession number: Q5PHC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program