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A4QEV1 (DAPF_CORGB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:cgR_1773
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length277 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 – 277277Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011872

Regions

Region83 – 853Substrate binding By similarity
Region212 – 2132Substrate binding By similarity
Region222 – 2232Substrate binding By similarity

Sites

Active site831Proton donor/acceptor By similarity
Active site2211Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site481Substrate By similarity
Binding site741Substrate By similarity
Binding site1591Substrate By similarity
Binding site1941Substrate By similarity
Site1611Important for catalytic activity By similarity
Site2121Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond83 ↔ 221 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A4QEV1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: A540184C69079066

FASTA27729,260
        10         20         30         40         50         60 
MNLTIPFAKG HATENDFIII PDEDARLDLT PEMVVKLCDR RAGIGADGIL RVVKAADVEG 

        70         80         90        100        110        120 
STVDPSLWFM DYRNADGSLA EMCGNGVRLF AHWLYSRSLV DNTSFDIGTR AGVRHVDILQ 

       130        140        150        160        170        180 
ADQHSAQVRV DMGIPDVTGL STCDINGQVF AGLGVDMGNP HLACVVPGLS ASALADMELR 

       190        200        210        220        230        240 
APTFDQEFFP HGVNVEIVTE LEDDAVSMRV WERGVGETRS CGTGTVAAAC AALADAGLGE 

       250        260        270 
GTVKVCVPGG EVEVQIFDDG STLTGPSAII ALGEVQI 

« Hide

References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009044 Genomic DNA. Translation: BAF54767.1.
RefSeqYP_001138669.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QEV1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340322.cgR_1773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF54767; BAF54767; cgR_1773.
GeneID4994319.
KEGGcgt:cgR_1773.
PATRIC21508156. VBICorGlu58097_1825.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycCGLU340322:GJBE-1853-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_CORGB
AccessionPrimary (citable) accession number: A4QEV1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 46 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