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C1KWW2 (DAPF_LISMC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:Lm4b_02030
OrganismListeria monocytogenes serotype 4b (strain CLIP80459) [Complete proteome] [HAMAP]
Taxonomic identifier568819 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length329 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 – 329329Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000204063

Regions

Region82 – 843Substrate binding By similarity
Region224 – 2252Substrate binding By similarity
Region234 – 2352Substrate binding By similarity

Sites

Active site821Proton donor/acceptor By similarity
Active site2331Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site531Substrate By similarity
Binding site731Substrate By similarity
Binding site1701Substrate By similarity
Binding site2061Substrate By similarity
Site1721Important for catalytic activity By similarity
Site2241Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond82 ↔ 233 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
C1KWW2 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 5209E21E5F43C0A6

FASTA32936,227
        10         20         30         40         50         60 
METIHFTKVH GSQNDFFLVD EEENHITEWS DEKRANFAIK LCDRKHSLGG ADGILYVTKS 

        70         80         90        100        110        120 
SEVGPIGQMR VVNSDGSIAS MCGNGLRTVA RYLLEKHALT DAKVETMKAI LDVKKATSLG 

       130        140        150        160        170        180 
FDIPTYQVEI SPVKFAAETL PMHVGVEKLF NQVIPELDAE LAFSAVSVPN PHLITFVDQA 

       190        200        210        220        230        240 
VLDSNKQEKL ASYLNSENPY FPDGVNVSFV KRLSDDAIYV RTFERGVGFT NACGTAMSAC 

       250        260        270        280        290        300 
SLIKKMLDND ILETPLNVYN DGGRVQVTAK KDAAGEISLQ LIGNATFVSK GSVRYENDVV 

       310        320 
TELTNEATDE QGQYQALVKE VKEFLKTTE 

« Hide

References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIP80459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM242711 Genomic DNA. Translation: CAS05788.1.
RefSeqYP_002758722.1. NC_012488.1.

3D structure databases

ProteinModelPortalC1KWW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634178.Lm4b_02030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS05788; CAS05788; Lm4b_02030.
GeneID7703974.
KEGGlmc:Lm4b_02030.
PATRIC20307297. VBILisMon88360_2047.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000220466.
KOK01778.
OMAKDITVMV.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycLMON568819:GJF9-2999-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_LISMC
AccessionPrimary (citable) accession number: C1KWW2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 37 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