Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1JSH5 (DAPE_YERPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinyl-diaminopimelate desuccinylase

Short name=SDAP desuccinylase
EC=3.5.1.18
Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Gene names
Name:dapE
Ordered Locus Names:YPK_1372
OrganismYersinia pseudotuberculosis serotype O:3 (strain YPIII) [Complete proteome] [HAMAP]
Taxonomic identifier502800 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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

Catalytic activity

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

Cofactor

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

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

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01690

Sequence similarities

Belongs to the peptidase M20A family. DapE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690
PRO_0000375802

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B1JSH5 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: B42DD7FF83E3C679

FASTA37540,933
        10         20         30         40         50         60 
MICPVIELAQ QLIKRPSLSP SDAGCQEIMI QRLAAIGFTI EPMNFGDTLN FWAWRGEGET 

        70         80         90        100        110        120 
LAFAGHTDVV PTGDESHWHS PPFEPTIRDG MLYGRGAADM KGSLAAMIVA AERFVAAHPD 

       130        140        150        160        170        180 
HKGRLAFMIT SDEEAKATNG TVKVVEALMA RHERLDYCLV GEPSSTDRVG DIVKNGRRGS 

       190        200        210        220        230        240 
ITANLRIHGV QGHVAYPHLA DNPVHRAMPA LNELVATQWD EGNAFFPATS MQIANLQAGT 

       250        260        270        280        290        300 
GSNNVIPGEF YVQFNFRFST ELTDSLIKQR VAALLDRHQL DYTLEWVLSG QPFLTAKGAL 

       310        320        330        340        350        360 
VDAVVNAVKH YTEITPQLLT TGGTSDGRFI ALMGAQVVEL GPVNATIHKV NECVSAADLQ 

       370 
LLSRMYQKIM EQLIA 

« Hide

References

[1]"Complete sequence of Yersinia pseudotuberculosis YPIII."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YPIII.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000950 Genomic DNA. Translation: ACA67666.1.
RefSeqYP_001720119.1. NC_010465.1.

3D structure databases

ProteinModelPortalB1JSH5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING502800.YPK_1372.

Protein family/group databases

MEROPSM20.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA67666; ACA67666; YPK_1372.
GeneID6089141.
KEGGypy:YPK_1372.
PATRIC18659920. VBIYerPse127545_1456.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243770.
KOK01439.
OMANECVHAA.
OrthoDBEOG60651W.
ProtClustDBPRK13009.

Enzyme and pathway databases

BioCycYPSE502800:GH0W-1386-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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPE_YERPY
AccessionPrimary (citable) accession number: B1JSH5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways