Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A6K2 (DAPF_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:Z5326, ECs4739
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length274 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.

Sequence caution

The sequence AAG59002.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB38162.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 274274Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149839

Regions

Region8 – 92Substrate binding By similarity
Region73 – 753Substrate binding By similarity
Region208 – 2092Substrate binding By similarity

Sites

Active site731Proton donor/acceptor By similarity
Active site2171Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site641Substrate By similarity
Binding site1571Substrate By similarity
Binding site1901Substrate By similarity
Site1591Important for catalytic activity By similarity
Site2081Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond73 ↔ 217 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
P0A6K2 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 4ACC137D2F5BD240

FASTA27430,209
        10         20         30         40         50         60 
MQFSKMHGLG NDFMVVDAVT QNVFFSPELI RRLADRHLGV GFDQLLVVEP PYDPELDFHY 

        70         80         90        100        110        120 
RIFNADGSEV AQCGNGARCF ARFVRLKGLT NKRDIRVSTA NGRMVLTVTD DDLVRVNMGE 

       130        140        150        160        170        180 
PNFEPSAVPF RANKAEKTYI MRAAEQTILC GVVSMGNPHC VIQVDDVDTA AVETLGPVLE 

       190        200        210        220        230        240 
SHERFPERAN IGFMQVVKRE HIRLRVYERG AGETQACGSG ACAAVAVGIQ QGLLAEEVRV 

       250        260        270 
ELPGGRLDIA WKGPGHPLYM TGPAVHVYDG FIHL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG59002.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB38162.1. Different initiation.
RefSeqNP_290438.2. NC_002655.2.
NP_312766.2. NC_002695.1.

3D structure databases

ProteinModelPortalP0A6K2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1228007.
STRING155864.Z5326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG59002; AAG59002; Z5326.
BAB38162; BAB38162; BAB38162.
GeneID915186.
960353.
KEGGece:Z5326.
ecs:ECs4739.
PATRIC18359099. VBIEscCol44059_4704.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycECOL386585:GJFA-4721-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_ECO57
AccessionPrimary (citable) accession number: P0A6K2
Secondary accession number(s): P08885, P78126, Q8X8P8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 11, 2014
This is version 62 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