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Q65FD6 (DAPF_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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:BLi03399, BL03150
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length285 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 – 285285Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011843

Regions

Region11 – 122Substrate binding By similarity
Region76 – 783Substrate binding By similarity
Region217 – 2182Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2261Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site491Substrate By similarity
Binding site671Substrate By similarity
Binding site1661Substrate By similarity
Binding site1991Substrate By similarity
Site1681Important for catalytic activity By similarity
Site2171Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 226 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q65FD6 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: ED63E989BEA1C799

FASTA28531,268
        10         20         30         40         50         60 
MNSFRFTKMH GLGNSYIYVN QFEEHLPEEL LSDLAVKVSS VYTGIGSDGM ILICPSDRAP 

        70         80         90        100        110        120 
VKMRIFNSDG SEGKNCGNGL RCVAKYAYEH KLVEETSFLI ETLSGLVKAQ VEVDEGKVVS 

       130        140        150        160        170        180 
ATVDMGEPRL LKSDMPMRGE QGSETINEKM IFGGREMKGT AVSMGNPHIV FYLDDIEKAP 

       190        200        210        220        230        240 
LTTMGPLIEK DERFPEGVNV EFVEVENENE LHFRVWERGS GITQACGTGA CAAAVSSVLN 

       250        260        270        280 
GYSKRDTDIT VHLAGGDLII NWKNDGRVMM TGPAETVCEG EFFIS 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU24860.1.
AE017333 Genomic DNA. Translation: AAU42228.1.
RefSeqYP_006714695.1. NC_006322.1.
YP_080498.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65FD6.
SMRQ65FD6. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL03150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU24860; AAU24860; BL03150.
AAU42228; AAU42228; BLi03399.
GeneID3027547.
3099737.
KEGGbld:BLi03399.
bli:BL03150.
PATRIC18952544. VBIBacLic203714_3448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3362-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689. PTHR31689. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPF_BACLD
AccessionPrimary (citable) accession number: Q65FD6
Secondary accession number(s): Q62QV0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: June 11, 2014
This is version 73 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