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Q5HSQ5 (DAPF_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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:CJE1702
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [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
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_1000011866

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
Q5HSQ5 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 0F9B7FBF4509BABF

FASTA24928,349
        10         20         30         40         50         60 
MKFYKYCASG NDFVITNADR KEDRSALAKE LCNRYEGIGG DGFIVILPHE KYDFEWEFYN 

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

       130        140        150        160        170        180 
TFEELGKTWQ LCDTGVPHLV HFCQNLDEFD TILCQKMRQK YNANVNFVKI LDENHLKVRT 

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


CFEANYNFS 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW36132.1.
RefSeqYP_179680.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HSQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1702.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW36132; AAW36132; CJE1702.
GeneID3232329.
KEGGcjr:CJE1702.
PATRIC20045202. VBICamJej134361_1713.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMADETHEIH.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1732-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_CAMJR
AccessionPrimary (citable) accession number: Q5HSQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 57 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