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B2JJY4 (DAPF_BURP8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 43. 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:Bphy_0076
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length286 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 – 286286Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099222

Regions

Region75 – 773Substrate binding By similarity
Region217 – 2182Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2261Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1661Substrate By similarity
Binding site1991Substrate By similarity
Site1681Important for catalytic activity By similarity
Site2171Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 226 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B2JJY4 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 79FD072E1C848D9D

FASTA28630,870
        10         20         30         40         50         60 
MKLKFTKMHG AGNDFVVLDG YTQPLNLTET QVRALANRHF GVGADQLLVV EKPTVDGVDF 

        70         80         90        100        110        120 
RYRIFNCDGG EVEHCGNGAR CFVKFVRDSR LTDKRSVRVQ VQKGVITLTM QDNGEVVVDM 

       130        140        150        160        170        180 
GAPVFEPVQV PFDASGVEAR REGNDTLYAL EVNGETRWVS VVSMGNPHAV QVVDDVEAFP 

       190        200        210        220        230        240 
VLVDGPVIET HPRFPQRVNA GFMQIVGRSE VKLRVYERGA GETLACGTGA CAAVAAGIRR 

       250        260        270        280 
GLLDAPVKVH THGGTLTITW NGESASSLMM AGPAATVFEG EIELAD 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17167 / STM815.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001043 Genomic DNA. Translation: ACC69271.1.
RefSeqYP_001856317.1. NC_010622.1.

3D structure databases

ProteinModelPortalB2JJY4.
SMRB2JJY4. Positions 3-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391038.Bphy_0076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC69271; ACC69271; Bphy_0076.
GeneID6241580.
KEGGbph:Bphy_0076.
PATRIC19186239. VBIBurPhy25146_0079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKDITVMV.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycBPHY391038:GI4Z-78-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_BURP8
AccessionPrimary (citable) accession number: B2JJY4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 43 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