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Q5WZH5 (DAPF_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Diaminopimelate epimerase

Short name=DAP epimerase
EC=5.1.1.7
Gene names
Name:dapF
Ordered Locus Names:lpl0407
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan By similarity. HAMAP-Rule MF_00197

Catalytic activity

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. HAMAP-Rule MF_00197

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_00197

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197.

Sequence similarities

Belongs to the diaminopimelate epimerase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011896

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region211 – 2122Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2201Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1601Substrate By similarity
Binding site1931Substrate By similarity
Site1621Important for catalytic activity By similarity
Site2111Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 220 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q5WZH5 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: FE09025B958AE40C

FASTA27729,938
        10         20         30         40         50         60 
MGIKFTKMHG LGNDFIVLDG VNQSIQLTVE QIQKLANRHT GIGFDQCLLI ESSQTEGIDF 

        70         80         90        100        110        120 
NYRIFNADGQ EVGQCGNGAR CIALFARYYG LTAKNKLTVA TKTTLMDLII NEDNSVSVNM 

       130        140        150        160        170        180 
GVPRLAPGEI PLLADRQSPE YSLKLNNGNT VNLHAISVGN PHAVLLVENI DTAPVNSLGQ 

       190        200        210        220        230        240 
QISFHPQFPE QVNVGFMQIV NHEKINLRVY ERGCGETIAC GSGAVAAAAI ARLFYNLSDK 

       250        260        270 
ITVHLPGGDL CIQWPCPTAP IILTGPAAFV YEGTLLS 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH14637.1.
RefSeqYP_125773.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WZH5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl0407.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH14637; CAH14637; lpl0407.
GeneID3113320.
KEGGlpf:lpl0407.
PATRIC22314305. VBILegPne33733_0494.

Organism-specific databases

LegioListlpl0407.
CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-437-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPF_LEGPL
AccessionPrimary (citable) accession number: Q5WZH5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways