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C6UQ52 (C6UQ52_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690

Short name=SDAP desuccinylase HAMAP-Rule MF_01690
EC=3.5.1.18 HAMAP-Rule MF_01690
Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase HAMAP-Rule MF_01690
Gene names
Name:dapE HAMAP-Rule MF_01690 EMBL ACT73177.1
Ordered Locus Names:ECSP_3410 EMBL ACT73177.1
OrganismEscherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP] EMBL ACT73177.1
Taxonomic identifier544404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls By similarity. HAMAP-Rule MF_01690 SAAS SAAS005941

Catalytic activity

N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate. HAMAP-Rule MF_01690 SAAS SAAS005941

Cofactor

Binds 1 Co2+ ion per subunit By similarity. HAMAP-Rule MF_01690 SAAS SAAS005941

Binds 1 Zn2+ ion per subunit By similarity. HAMAP-Rule MF_01690 SAAS SAAS005941

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. HAMAP-Rule MF_01690 SAAS SAAS005941

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01690 SAAS SAAS005941

Sequence similarities

Belongs to the peptidase M20A family. DapE subfamily. HAMAP-Rule MF_01690

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site681 By similarity HAMAP-Rule MF_01690
Active site1331Proton acceptor By similarity HAMAP-Rule MF_01690
Metal binding661Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding991Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding991Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690
Metal binding1341Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690
Metal binding1621Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding3481Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690

Sequences

Sequence LengthMass (Da)Tools
C6UQ52 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: B249E6B09D84F2CA

FASTA37541,241
        10         20         30         40         50         60 
MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAIGFTV ERMDFADTQN FWAWRGQGET 

        70         80         90        100        110        120 
LAFAGHTDVV PPGDADRWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPN 

       130        140        150        160        170        180 
HTGRLAFLIT SDEEASAHNG TVKAVEALMA RNERLDYCLV GEPSSIEVVG DVVKNGRRGS 

       190        200        210        220        230        240 
LTCNLTIHGV QGHVAYPHLA DNPVHRAAPF LNELVAIEWD QGNEFFPATS MQIANIQAGT 

       250        260        270        280        290        300 
GSNNVIPGEL FVQFNFRFST ELTDEMIKAQ VLALLEKHQL RYTVDWWLSG QPFLTARGKL 

       310        320        330        340        350        360 
VDAVVNAVEH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVNAADLQ 

       370 
LLARMYQRIM EQLVA 

« Hide

References

[1]"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. expand/collapse author list , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW14359 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001368 Genomic DNA. Translation: ACT73177.1.
RefSeqYP_003079253.1. NC_013008.1.

3D structure databases

ProteinModelPortalC6UQ52.
SMRC6UQ52. Positions 2-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING544404.ECSP_3410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT73177; ACT73177; ECSP_3410.
GeneID8217976.
KEGGetw:ECSP_3410.
PATRIC18390894. VBIEscCol9396_3464.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243770.
KOK01439.
OMAHAGRLAF.
OrthoDBEOG60651W.

Enzyme and pathway databases

BioCycECOL544404:GKCX-3406-MONOMER.
UniPathwayUPA00034; UER00021.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
HAMAPMF_01690. DapE.
InterProIPR001261. ArgE/DapE_CS.
IPR005941. DapE_proteobac.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01246. dapE_proteo. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6UQ52_ECO5T
AccessionPrimary (citable) accession number: C6UQ52
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: June 11, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)