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A3MRQ6 (DAPF_BURM7) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:BMA10247_3426
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length289 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 – 289289Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011854

Regions

Region76 – 783Substrate binding By similarity
Region218 – 2192Substrate binding By similarity
Region228 – 2292Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2271Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site471Substrate By similarity
Binding site671Substrate By similarity
Binding site1671Substrate By similarity
Binding site2001Substrate By similarity
Site1691Important for catalytic activity By similarity
Site2181Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 227 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A3MRQ6 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 7A21ABF99D793D82

FASTA28930,899
        10         20         30         40         50         60 
MKLSFTKMHG AGNDFVVLDG YTRALPPLTG AQVRALADRH FGIGADQLLL VEKPTVDGAD 

        70         80         90        100        110        120 
FKYRIFNCDG GEVEHCGNGA RCFVKFVRDH GLTGKASVRV EVKHGVITLT MQDNGEVVVD 

       130        140        150        160        170        180 
MGAPVFEPAR VPFDASGLDG RREGADTLWP LPVNGVTRWI SVVSMGNPHA VQIVDDAEAF 

       190        200        210        220        230        240 
AVRVDGPAIE RDPRFPQRVN AGFMQIVSRH EVNLRVYERG AGETLACGTG ACAAVAAGIR 

       250        260        270        280 
RGRLDSPVTV HTHGGTLTIS WNGACDERAP LMMAGPATTV FEGVIELPA 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10247.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000548 Genomic DNA. Translation: ABO06804.1.
RefSeqYP_001082942.1. NC_009080.1.

3D structure databases

ProteinModelPortalA3MRQ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320389.BMA10247_3426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO06804; ABO06804; BMA10247_3426.
GeneID4892123.
KEGGbmn:BMA10247_3426.
PATRIC19149165. VBIBurMal96640_5610.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKDITVMV.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycBMAL320389:GH97-3410-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_BURM7
AccessionPrimary (citable) accession number: A3MRQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 50 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