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A7ML10 (DAPE_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:ESA_00778
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

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_0000375548

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
A7ML10 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 5F4EB07003167BEF

FASTA37541,244
        10         20         30         40         50         60 
MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAVGFTV EPMNIGDTQN FWAWRGTGET 

        70         80         90        100        110        120 
LAFAGHTDVV PAGDVERWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPH 

       130        140        150        160        170        180 
HRGRLAFLIT SDEEASATNG TVKVVEALMA RGERLDYCLV GEPSSSEVVG DVVKNGRRGS 

       190        200        210        220        230        240 
LTCNLTIHGV QGHVAYPHLA DNPVHRAAPM LNELVGIEWD RGNEFFPPTS MQIANIQAGT 

       250        260        270        280        290        300 
GSNNVIPGDL HVQFNFRFST ELTDEMIKQR VVALLEKYQL RYTLDWWLSG QPFLTARGKL 

       310        320        330        340        350        360 
VDAVVNAVHH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVKASDLQ 

       370 
LLARMYQRIM EQLVA 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU76055.1.
RefSeqYP_001436891.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7ML10.
SMRA7ML10. Positions 4-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290339.ESA_00778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU76055; ABU76055; ESA_00778.
GeneID5550571.
KEGGesa:ESA_00778.
PATRIC20393765. VBICroSak107175_0690.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243770.
KOK01439.
OMAEPMNIGD.
OrthoDBEOG60651W.

Enzyme and pathway databases

BioCycCSAK290339:GJ80-772-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 nameDAPE_CROS8
AccessionPrimary (citable) accession number: A7ML10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: October 2, 2007
Last modified: May 14, 2014
This is version 46 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