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B5Z6T7 (DAPF_HELPG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 41. 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:HPG27_525
OrganismHelicobacter pylori (strain G27) [Complete proteome] [HAMAP]
Taxonomic identifier563041 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length272 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 – 272272Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099240

Regions

Region69 – 713Substrate binding By similarity
Region199 – 2002Substrate binding By similarity
Region210 – 2112Substrate binding By similarity

Sites

Active site691Proton donor/acceptor By similarity
Active site2091Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site421Substrate By similarity
Binding site601Substrate By similarity
Binding site1811Substrate By similarity
Site1521Important for catalytic activity By similarity
Site1991Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond69 ↔ 209 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B5Z6T7 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 5B584BAE95D993DF

FASTA27230,566
        10         20         30         40         50         60 
MVFYKYSGSG NDFLITQSFK KKDFSNLAKQ VCHRHEGFGA DGLVVVLPSK DYDYEWDFYN 

        70         80         90        100        110        120 
SDGSKAGMCG NASRCVGLFA YQHAIAPKEH VFLAGKREIS IRIEEPNIIE SNLGNYKILD 

       130        140        150        160        170        180 
TIPALRCKKF FTNDSVLENI LTFYLIDTGV PHLVGFVKNK KLLNSLNTLE LRALRHEFNA 

       190        200        210        220        230        240 
NINIAFIENK ETIFLQTYER GVEDFTLACG TGMAAVFIAS HIFYNTPKKA ILIPKSNESL 

       250        260        270 
ELSLKNDGIF YKGAVRYIGM SVLGSVFENG CF 

« Hide

References

[1]"The complete genome sequence of Helicobacter pylori strain G27."
Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S., Ottemann K.M., Stein M., Salama N.R., Guillemin K.
J. Bacteriol. 191:447-448(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001173 Genomic DNA. Translation: ACI27286.1.
RefSeqYP_002266152.1. NC_011333.1.

3D structure databases

ProteinModelPortalB5Z6T7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING563041.HPG27_525.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI27286; ACI27286; HPG27_525.
GeneID6963414.
KEGGhpg:HPG27_525.
PATRIC20599021. VBIHelPyl113476_0566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAVFDRYFL.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycHPYL563041:GC38-537-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_HELPG
AccessionPrimary (citable) accession number: B5Z6T7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: June 11, 2014
This is version 41 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