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B2T1P5 (DAPF_BURPP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Bphyt_0349
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length299 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 – 299299Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099223

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
B2T1P5 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 9A7B1DD5276F2944

FASTA29932,046
        10         20         30         40         50         60 
MKLKFTKMHG AGNDFVVLDG YTQPVNLTPA QVRALADRHF GVGADQLLLV EKPTVAGVDF 

        70         80         90        100        110        120 
RYRIFNCDGG EVEHCGNGAR CFVKFVRDSG LTDQRSVRVQ VQKGTITLTM QENGEVLVDM 

       130        140        150        160        170        180 
GTPVFDPERV PFATKGLQGR GEGADTLWPL DVNGTTRWIS VVSMGNPHAV QVVDDVEAFP 

       190        200        210        220        230        240 
VLVEGPVIER HARFPQRVNA GFMQIVGRSE IKLRVYERGA GETLACGTGA CAAVAAGIRR 

       250        260        270        280        290 
GLLDAPVLVH THGGKLTITW DAAQADQPLL MAGPAATVFE GEIELPDSLA DSLANSQAA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001052 Genomic DNA. Translation: ACD14774.1.
RefSeqYP_001893998.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2T1P5.
SMRB2T1P5. Positions 3-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398527.Bphyt_0349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD14774; ACD14774; Bphyt_0349.
GeneID6281342.
KEGGbpy:Bphyt_0349.
PATRIC19210537. VBIBurPhy117947_4060.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycBPHY398527:GJEX-350-MONOMER.
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_BURPP
AccessionPrimary (citable) accession number: B2T1P5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 40 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