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Q9ZLR5 (DAPF_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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:jhp_0513
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length273 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 – 273273Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149844

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
Q9ZLR5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C63F468B833841D8

FASTA27330,661
        10         20         30         40         50         60 
MVFYKYSGSG NDFLITQSFK KKDFSNLAQQ VCHRHEGFGA DGLVVVLPSK DYDYEWDFYN 

        70         80         90        100        110        120 
SDGSKAGMCG NASRCVGLFA YQHAIAPKEH VFLAGKREIS IRIEEPNIVE SNLGNYQILD 

       130        140        150        160        170        180 
TIPNLRCKKF FTNNSVLENI PMFYLINTGV PHLVGFVKNK GLLNSLNTLE LRALRHEFNA 

       190        200        210        220        230        240 
NINIAFIENK ETIFLQTYER GVEDFTLACG TGMAAVFIAA RLFHNTPKKA TLIPKSNEFL 

       250        260        270 
ELSLKNDGIF YKGVARYIGM SVLGMGVFKN GCF 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06089.1.
PIRG71923.
RefSeqNP_223231.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZLR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp0513.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06089; AAD06089; jhp_0513.
GeneID889270.
KEGGhpj:jhp0513.
PATRIC20605716. VBIHelPyl98156_0564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMAVFDRYFL.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-524-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZLR5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 85 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