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Q8YJF0 (DAPF_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BMEI0133
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length303 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 – 303303Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149823

Regions

Region12 – 132Substrate binding By similarity
Region76 – 783Substrate binding By similarity
Region215 – 2162Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2241Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site471Substrate By similarity
Binding site671Substrate By similarity
Binding site1631Substrate By similarity
Binding site1971Substrate By similarity
Site1651Important for catalytic activity By similarity
Site2151Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 224 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q8YJF0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 6C9FD0D4A9C0AA48

FASTA30332,368
        10         20         30         40         50         60 
MATKAAFARM NGLGNQIIVA DMRGRADSIT SAAAIRLASD SETAFDQIMA IHDPRTPGTD 

        70         80         90        100        110        120 
YYIAIINCDG TQAQACGNGT RCVVQALAAE TGRHAFTFET RAGILTATEH DDGLISVDMG 

       130        140        150        160        170        180 
TPRFDWQDIP LAQAVADTRK IELQVDPADA PVLHSPSIAS MGNPHAVFWV DKDVWSYELD 

       190        200        210        220        230        240 
KFGPLLENHP IFPERANISI AHVTSSDTID LRTWERGAGL TRACGSAACA AAVSAARTGR 

       250        260        270        280        290        300 
TGRKVTVNVP GGPLLIEWRD DDHVMMTGPA EWEFSGTFDP ATGEWSRDTQ GLQGSGNADR 


GAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008917 Genomic DNA. Translation: AAL51315.1.
PIRAH3268.
RefSeqNP_539051.1. NC_003317.1.

3D structure databases

ProteinModelPortalQ8YJF0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224914.BMEI0133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL51315; AAL51315; BMEI0133.
GeneID1195845.
KEGGbme:BMEI0133.
PATRIC17795413. VBIBruMel146950_0873.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000220466.
KOK01778.
OMAFMRIYNT.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

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_BRUME
AccessionPrimary (citable) accession number: Q8YJF0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 71 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

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names