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Q9PMD8 (DAPF_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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:Cj1531
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length249 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
Reference 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 – 249249Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149828

Regions

Region69 – 713Substrate binding By similarity
Region182 – 1832Substrate binding By similarity
Region193 – 1942Substrate binding By similarity

Sites

Active site691Proton donor/acceptor By similarity
Active site1921Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site421Substrate By similarity
Binding site601Substrate By similarity
Binding site1641Substrate By similarity
Site1381Important for catalytic activity By similarity
Site1821Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond69 ↔ 192 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q9PMD8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C6CA06E673F17348

FASTA24928,410
        10         20         30         40         50         60 
MKFYKYCASG NDFVITNADR KEDRSALAKE LCNRYEGIGA DGFIVILPHE KYDFEWEFYN 

        70         80         90        100        110        120 
NDGSRAAMCG NGSRAAAHFA HHINKINPNM SFLTGAGIIK AKVNQDKVEV SLGKIKSVQN 

       130        140        150        160        170        180 
TFEELGKTWQ LCNTGVPHLV HFCQNLDEFD TMLCQKMRQK YNANVNFVKI LDENHLKVRT 

       190        200        210        220        230        240 
YERGVEDETL ACGTGMGACF YLAFLNKKVQ NKVKITPKSG EEVGFAYKNE ELFFEGKVKY 


CFEANYNFF 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35631.1.
PIRA81300.
RefSeqYP_002344903.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PMD8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192222.Cj1531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35631; CAL35631; Cj1531.
GeneID905812.
KEGGcje:Cj1531.
PATRIC20060022. VBICamJej33762_1508.

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAINTGSPH.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1493-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_CAMJE
AccessionPrimary (citable) accession number: Q9PMD8
Secondary accession number(s): Q0P894
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 76 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