Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C3PNE1 (DAPF_RICAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:RAF_ORF0540
OrganismRickettsia africae (strain ESF-5) [Complete proteome] [HAMAP]
Taxonomic identifier347255 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length270 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 – 270270Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000204066

Regions

Region12 – 132Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region204 – 2052Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2131Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site491Substrate By similarity
Binding site661Substrate By similarity
Binding site1551Substrate By similarity
Binding site1871Substrate By similarity
Site1571Important for catalytic activity By similarity
Site2041Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 213 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
C3PNE1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 78A2F36293D0FE53

FASTA27030,085
        10         20         30         40         50         60 
MISKINFVKM HGLGNDFVIV NKRDLSSSYD LSQLAKNMAE RHTGIGCDQF IIYEEHNDFY 

        70         80         90        100        110        120 
EMIIYNIDGS SAKLCGNATR CLAKLIYLDT GKQDITVMVG NKKLLCNVND ENNISVNVGS 

       130        140        150        160        170        180 
VSFNEAWMPN RDKVWEFAER YMIDLKETIC VDIGNPHVVI FSKLEPQDQK IVGERLQAKE 

       190        200        210        220        230        240 
LFADGVNVNF AEVKDNKIYL SVWERGAGLT LACGSGACGS FAAGLKRGFI HSPSTIVFKH 

       250        260        270 
GNLTMKEENG NIIMQGAATL VARGEYYCEQ 

« Hide

References

[1]"Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction."
Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.
BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ESF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001612 Genomic DNA. Translation: ACP53451.1.
RefSeqYP_002845194.1. NC_012633.1.

3D structure databases

ProteinModelPortalC3PNE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347255.RAF_ORF0540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP53451; ACP53451; RAF_ORF0540.
GeneID7814957.
KEGGraf:RAF_ORF0540.
PATRIC17873032. VBIRicAfr6986_0651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAFILDQTE.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycRAFR347255:GJCT-505-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 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_RICAE
AccessionPrimary (citable) accession number: C3PNE1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: February 19, 2014
This is version 35 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