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B1Y6S6 (DAPF_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:Lcho_0129
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesLeptothrix

Protein attributes

Sequence length297 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 – 297297Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099244

Regions

Region76 – 783Substrate binding By similarity
Region225 – 2262Substrate binding By similarity
Region235 – 2362Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2341Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1741Substrate By similarity
Binding site2071Substrate By similarity
Site1761Important for catalytic activity By similarity
Site2251Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 234 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B1Y6S6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 0F20436686B685E5

FASTA29732,011
        10         20         30         40         50         60 
MRLHFTKMQG AGNDFVVLDA TRAPLALSAA DYRFLGDRRF GVGADQILVV ERSTTPGVDF 

        70         80         90        100        110        120 
RYRIFNGGSG DEVEQCGNGA RCFARFVRDN GLSQQVRVKV ETVNSLIELH VEADGRVTVD 

       130        140        150        160        170        180 
MNQPIFEHAL IPFDSAGLSA RPHNGHGNGF ELWPLQLPGA SLPSVDVAVL SMGNPHAVQR 

       190        200        210        220        230        240 
VHDVDTAPVA EIGPRVETHA RFPRHVNAGF MQVMSRREVR LRVFERGAGE TLACGTGACA 

       250        260        270        280        290 
AVVAGIRLGW LDPEVDVQTR GGLLTIAWAG LGHPVLMTGP AQTVFTGDID LPTTSVQ 

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB32404.1.
RefSeqYP_001789169.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y6S6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395495.Lcho_0129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB32404; ACB32404; Lcho_0129.
GeneID6162710.
KEGGlch:Lcho_0129.
PATRIC22390527. VBILepCho83238_0133.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycLCHO395495:GHYL-129-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPF_LEPCP
AccessionPrimary (citable) accession number: B1Y6S6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 41 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