Succinylglutamate desuccinylase - Escherichia coli (strain K12)

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P76215 (ASTE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Succinylglutamate desuccinylase
EC=3.5.1.96

Gene names

Name:	astE
Synonyms:	ydjS
Ordered Locus Names:	b1744, JW1733

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transforms N(2)-succinylglutamate into succinate and glutamate. Ref.4
Catalytic activity	N-succinyl-L-glutamate + H₂O = succinate + L-glutamate. HAMAP-Rule MF_00767
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00767
Pathway	Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. HAMAP-Rule MF_00767
Induction	By nitrogen starvation, and arginine. Induced at stationary phase by sigma S. Ref.6
Sequence similarities	Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.

Ontologies

Keywords
Biological process	Arginine metabolism Stress response
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference 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 response to stress Inferred from electronic annotation. Source: UniProtKB-KW
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_0000174639

Sites

Active site

210

Potential

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

147

Zinc By similarity

Secondary structure

322

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P76215 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 6602BAD75AB0A893
Show »

FASTA

322

35,800

        10         20         30         40         50         60 
MDNFLALTLT GKKPVITERE INGVRWRWLG DGVLELTPLT PPQGALVISA GIHGNETAPV 

        70         80         90        100        110        120 
EMLDALLGAI SHGEIPLRWR LLVILGNPPA LKQGKRYCHS DMNRMFGGRW QLFAESGETC 

       130        140        150        160        170        180 
RARELEQCLE DFYDQGKESV RWHLDLHTAI RGSLHPQFGV LPQRDIPWDE KFLTWLGAAG 

       190        200        210        220        230        240 
LEALVFHQEP GGTFTHFSAR HFGALACTLE LGKALPFGQN DLRQFAVTAS AIAALLSGES 

       250        260        270        280        290        300 
VGIVRTPPLR YRVVSQITRH SPSFEMHMAS DTLNFMPFEK GTLLAQDGEE RFTVTHDVEY 

       310        320 
VLFPNPLVAL GLRAGLMLEK IS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells." Hagenmaier S., Stierhof Y.-D., Henning U. J. Bacteriol. 179:2073-2076(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-322. Strain: K12.
[4]	"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli." Schneider B.L., Kiupakis A.K., Reitzer L.J. J. Bacteriol. 180:4278-4286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"The Zn-peptidase superfamily: functional convergence after evolutionary divergence." Makarova K.S., Grishin N.V. J. Mol. Biol. 292:11-17(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PREDICTION OF ZINC-BINDING RESIDUES AND ACTIVE SITE.
[6]	"ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli." Kiupakis A.K., Reitzer L. J. Bacteriol. 184:2940-2950(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[7]	"Crystal structure of succinylglutamate desuccinylase from Escherichia coli, Northeast structural genomics target Et72." Northeast structural genomics consortium (NESG) Submitted (MAY-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC74814.1.
AP009048 Genomic DNA. Translation: BAE76515.1.

PIR

H64933.

RefSeq

NP_416258.1. NC_000913.2.
YP_490005.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YW6	X-ray	3.10	A/B	1-322	[»]

ProteinModelPortal

P76215.

SMR

P76215. Positions 1-322.

ModBase

Search...

Protein-protein interaction databases

IntAct

P76215. 5 interactions.

STRING

511145.b1744.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74814; AAC74814; b1744.
BAE76515; BAE76515; BAE76515.

GeneID

12933245.
946256.

KEGG

ecj:Y75_p1719.
eco:b1744.

PATRIC

32118797. VBIEscCol129921_1816.

Organism-specific databases

EchoBASE

EB3751.

EcoGene

EG13995. astE.

Phylogenomic databases

eggNOG

COG2988.

HOGENOM

HOG000280300.

K05526.

OMA

TAPIEIC.

ProtClustDB

PRK05324.

Enzyme and pathway databases

BioCyc

EcoCyc:SUCCGLUDESUCC-MONOMER.
ECOL316407:JW1733-MONOMER.
MetaCyc:SUCCGLUDESUCC-MONOMER.

UniPathway

UPA00185; UER00283.

Gene expression databases

Genevestigator

P76215.

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...

Other

EvolutionaryTrace

P76215.

Entry information

Entry name

ASTE_ECOLI

Accession

Primary (citable) accession number: P76215
Secondary accession number(s): Q2MB41

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents