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Q9PH30 (DAPE_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:XF_0116
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length377 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 MF_01690

Catalytic activity

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

Cofactor

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

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

Subunit structure

Homodimer By similarity. HAMAP MF_01690

Sequence similarities

Belongs to the peptidase M20A family. DapE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Succinyl-diaminopimelate desuccinylase HAMAP MF_01690
PRO_0000375789

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
Q9PH30 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1FB7EDA4ACA2E6B8

FASTA37740,723
        10         20         30         40         50         60 
MSEVFDLTCD LISRPSVTPE DAGCQAMIAA RLERVGFTCE HLHYGSVANL WATHGQGAPV 

        70         80         90        100        110        120 
LVLLGHTDVV PPGPIEAWTS DPFIPQRREG KLYGRGAADM KGSVAAFVIA AERFLVAHAG 

       130        140        150        160        170        180 
HPGTLAILLT SDEEGQAIDG VRKVAETLRQ RGQGIDWCLT GEPSSSKRLG DLLRVGRRGS 

       190        200        210        220        230        240 
LSATLHVKGV QGHVAYPHQA RNPIHLAVPA LAALTARHWD DGDESFPSTS LQISNIHAGT 

       250        260        270        280        290        300 
GANNVIPGAL EVAFNLRYNP HWSAPRLESE IVALLDQHGL DYTLHWHRSG EPFYTPEGKL 

       310        320        330        340        350        360 
RRIAREVLER FSGAPPEEST GGGTSDARFI APLGAQCIEI GPVNASIHQV DEHVCLADLE 

       370 
ALPDLYQLLI ERLLADH

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003849 Genomic DNA. Translation: AAF82929.1.
PIRB82846.
RefSeqNP_297409.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PH30.
SMRQ9PH30. Positions 2-374.
ModBaseSearch...

Protein family/group databases

MEROPSM20.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1125633.
GenomeReviewsGene locus XF_0116 in contig AE003849_GR.
KEGGxfa:XF0116.
NMPDRfig|160492.1.peg.116.
PATRIC24130126. VBIXylFas578_0120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG728841.
OMAPMVFEDT.
ProtClustDBPRK13009.

Enzyme and pathway databases

BioCycXFAS160492:XF0116-MONOMER.

Family and domain databases

HAMAPMF_01690. DapE.
[Tree]
InterProIPR001261. ArgE/DapE_CS.
IPR005941. DapE_proteobac.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
KOK01439.
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMSSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMsTIGR01246. DapE_proteo. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. False negative.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPE_XYLFA
AccessionPrimary (citable) accession number: Q9PH30
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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