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Q8FPE1 (DAPF_COREF) 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:CE1837
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length283 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.

Sequence caution

The sequence BAC18647.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 283283Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149836

Regions

Region85 – 873Substrate binding By similarity
Region218 – 2192Substrate binding By similarity
Region228 – 2292Substrate binding By similarity

Sites

Active site851Proton donor/acceptor By similarity
Active site2271Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site481Substrate By similarity
Binding site761Substrate By similarity
Binding site1611Substrate By similarity
Binding site1961Substrate By similarity
Site1631Important for catalytic activity By similarity
Site2181Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond85 ↔ 227 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q8FPE1 [UniParc].

Last modified April 11, 2003. Version 2.
Checksum: CF9C66BA14E02F94

FASTA28329,564
        10         20         30         40         50         60 
MKKEIAFAKG HATENDFIII HDPDGTIDLT ADEVTRLCDR RAGLGADGVL RVVRAGELGV 

        70         80         90        100        110        120 
QTPGVDPGWW FMDYRNADGS LAEMCGNGVR VFAHWLAAHQ LVDTTDFTIG TRAGARSVTV 

       130        140        150        160        170        180 
LSADRDDAVV RVDMGPAAVT GISTCMIADQ PFAGMGVDLG NPHLACVVPG LTPAALKNIA 

       190        200        210        220        230        240 
LEAPVFDTAF FPRGVNVELV TELADGLDDP AIHMRVWERG VGETRSCGTG TVAAARAALA 

       250        260        270        280 
DAGQAVGTVT VYVPGGAVEV GIREETSTLT GPSRIIATGT VRI 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18647.1. Different initiation.
RefSeqNP_738447.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FPE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE1837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18647; BAC18647; BAC18647.
GeneID1034484.
KEGGcef:CE1837.
PATRIC21489827. VBICorEff9312_1827.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000220467.
KOK01778.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycCEFF196164:GJW8-1873-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_COREF
AccessionPrimary (citable) accession number: Q8FPE1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: April 11, 2003
Last modified: February 19, 2014
This is version 63 of the entry and version 2 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