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Q6G1L7 (DAPF_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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:BH16600
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length283 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 – 283283Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011846

Regions

Region10 – 112Substrate binding By similarity
Region74 – 763Substrate binding By similarity
Region208 – 2092Substrate binding By similarity

Sites

Active site741Proton donor/acceptor By similarity
Active site2171Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site451Substrate By similarity
Binding site651Substrate By similarity
Binding site1561Substrate By similarity
Binding site1901Substrate By similarity
Site1581Important for catalytic activity By similarity
Site2081Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond74 ↔ 217 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q6G1L7 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: BFCBCE335EEB9F34

FASTA28331,224
        10         20         30         40         50         60 
MKTPFSKMDG LGNQIIVADM RESTHALTPQ AILSLAADSQ TYFDQIMAIH LPTKKEADFR 

        70         80         90        100        110        120 
IEIWNADGSM ANACGNGTRC VIAWLTDHNY GEIFRLETPA GIVEGKRQID NLISVDMGCP 

       130        140        150        160        170        180 
NFNAKEMPVS REIIDTNHVE LTAGPLRDAC LVSIGNLHAI FFVENDIQYI PLEKYGSKLE 

       190        200        210        220        230        240 
HDPLFPQRCN ISIACVTSQE SLNLRTWERG AGLTQACGSA ACASAVAAYR RGLTKRNIDV 

       250        260        270        280 
NLPGGTLNIF YREDDHIIMT GPVKYGFSGF LNPLTGSYKK DDF 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF28421.1.
RefSeqYP_034350.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ6G1L7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283166.BH16600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF28421; CAF28421; BH16600.
GeneID2864507.
KEGGbhe:BH16600.
PATRIC20547646. VBIBarHen29080_1930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycBHEN283166:GIVZ-1656-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_BARHE
AccessionPrimary (citable) accession number: Q6G1L7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: June 11, 2014
This is version 61 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