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Protein

Succinylglutamate desuccinylase

Gene

astE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transforms N(2)-succinylglutamate into succinate and glutamate.1 Publication

Catalytic activityi

N-succinyl-L-glutamate + H2O = succinate + L-glutamate.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathway: L-arginine degradation via AST pathway

This protein is involved in step 5 of the subpathway that synthesizes L-glutamate and succinate from L-arginine.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Arginine N-succinyltransferase (astA), Arginine N-succinyltransferase (astA)
  2. N-succinylarginine dihydrolase (astB), N-succinylarginine dihydrolase (astB)
  3. Succinylornithine transaminase (astC), Succinylornithine transaminase (astC)
  4. N-succinylglutamate 5-semialdehyde dehydrogenase (astD), N-succinylglutamate 5-semialdehyde dehydrogenase (astD)
  5. Succinylglutamate desuccinylase (astE), Succinylglutamate desuccinylase (astE)
This subpathway is part of the pathway L-arginine degradation via AST pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate and succinate from L-arginine, the pathway L-arginine degradation via AST pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531ZincBy similarity
Metal bindingi56 – 561ZincBy similarity
Metal bindingi147 – 1471ZincBy similarity
Active sitei210 – 2101Sequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Stress response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:SUCCGLUDESUCC-MONOMER.
ECOL316407:JW1733-MONOMER.
MetaCyc:SUCCGLUDESUCC-MONOMER.
BRENDAi3.5.1.96. 2026.
UniPathwayiUPA00185; UER00283.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinylglutamate desuccinylase (EC:3.5.1.96)
Gene namesi
Name:astE
Synonyms:ydjS
Ordered Locus Names:b1744, JW1733
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13995. astE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Succinylglutamate desuccinylasePRO_0000174639Add
BLAST

Expressioni

Inductioni

By nitrogen starvation, and arginine. Induced at stationary phase by sigma S.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
acrRP0ACS93EBI-1121806,EBI-1117360

Protein-protein interaction databases

IntActiP76215. 10 interactions.
STRINGi511145.b1744.

Structurei

Secondary structure

322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1010Combined sources
Beta strandi18 – 3013Combined sources
Beta strandi33 – 408Combined sources
Beta strandi45 – 506Combined sources
Beta strandi52 – 554Combined sources
Helixi58 – 7114Combined sources
Beta strandi79 – 846Combined sources
Helixi88 – 914Combined sources
Beta strandi105 – 1106Combined sources
Helixi117 – 13418Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi153 – 1619Combined sources
Helixi170 – 1789Combined sources
Beta strandi182 – 1865Combined sources
Helixi194 – 2018Combined sources
Beta strandi205 – 2106Combined sources
Helixi225 – 23612Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi249 – 2557Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi296 – 3027Combined sources
Beta strandi316 – 3216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YW6X-ray3.10A/B1-322[»]
ProteinModelPortaliP76215.
SMRiP76215. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76215.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2988.
HOGENOMiHOG000280300.
InParanoidiP76215.
KOiK05526.
OMAiFPNPNVA.
OrthoDBiEOG613070.

Family and domain databases

HAMAPiMF_00767. Arg_catab_AstE.
InterProiIPR007036. Aste_AspA.
IPR016681. SuccinylGlu_desuccinylase.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF017020. AstE. 1 hit.
TIGRFAMsiTIGR03242. arg_catab_astE. 1 hit.

Sequencei

Sequence statusi: Complete.

P76215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNFLALTLT GKKPVITERE INGVRWRWLG DGVLELTPLT PPQGALVISA
60 70 80 90 100
GIHGNETAPV EMLDALLGAI SHGEIPLRWR LLVILGNPPA LKQGKRYCHS
110 120 130 140 150
DMNRMFGGRW QLFAESGETC RARELEQCLE DFYDQGKESV RWHLDLHTAI
160 170 180 190 200
RGSLHPQFGV LPQRDIPWDE KFLTWLGAAG LEALVFHQEP GGTFTHFSAR
210 220 230 240 250
HFGALACTLE LGKALPFGQN DLRQFAVTAS AIAALLSGES VGIVRTPPLR
260 270 280 290 300
YRVVSQITRH SPSFEMHMAS DTLNFMPFEK GTLLAQDGEE RFTVTHDVEY
310 320
VLFPNPLVAL GLRAGLMLEK IS
Length:322
Mass (Da):35,800
Last modified:February 1, 1997 - v1
Checksum:i6602BAD75AB0A893
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74814.1.
AP009048 Genomic DNA. Translation: BAE76515.1.
PIRiH64933.
RefSeqiNP_416258.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74814; AAC74814; b1744.
BAE76515; BAE76515; BAE76515.
GeneIDi946256.
KEGGiecj:Y75_p1719.
eco:b1744.
PATRICi32118797. VBIEscCol129921_1816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74814.1.
AP009048 Genomic DNA. Translation: BAE76515.1.
PIRiH64933.
RefSeqiNP_416258.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YW6X-ray3.10A/B1-322[»]
ProteinModelPortaliP76215.
SMRiP76215. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP76215. 10 interactions.
STRINGi511145.b1744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74814; AAC74814; b1744.
BAE76515; BAE76515; BAE76515.
GeneIDi946256.
KEGGiecj:Y75_p1719.
eco:b1744.
PATRICi32118797. VBIEscCol129921_1816.

Organism-specific databases

EchoBASEiEB3751.
EcoGeneiEG13995. astE.

Phylogenomic databases

eggNOGiCOG2988.
HOGENOMiHOG000280300.
InParanoidiP76215.
KOiK05526.
OMAiFPNPNVA.
OrthoDBiEOG613070.

Enzyme and pathway databases

UniPathwayiUPA00185; UER00283.
BioCyciEcoCyc:SUCCGLUDESUCC-MONOMER.
ECOL316407:JW1733-MONOMER.
MetaCyc:SUCCGLUDESUCC-MONOMER.
BRENDAi3.5.1.96. 2026.

Miscellaneous databases

EvolutionaryTraceiP76215.
PROiP76215.

Family and domain databases

HAMAPiMF_00767. Arg_catab_AstE.
InterProiIPR007036. Aste_AspA.
IPR016681. SuccinylGlu_desuccinylase.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF017020. AstE. 1 hit.
TIGRFAMsiTIGR03242. arg_catab_astE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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).

Entry informationi

Entry nameiASTE_ECOLI
AccessioniPrimary (citable) accession number: P76215
Secondary accession number(s): Q2MB41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.