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A8GWH4 (DAPF_RICB8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 45. 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:A1I_04280
OrganismRickettsia bellii (strain OSU 85-389) [Complete proteome] [HAMAP]
Taxonomic identifier391896 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length269 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 – 269269Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011953

Regions

Region12 – 132Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region204 – 2052Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2131Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site491Substrate By similarity
Binding site661Substrate By similarity
Binding site1551Substrate By similarity
Binding site1871Substrate By similarity
Site1571Important for catalytic activity By similarity
Site2041Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 213 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A8GWH4 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 0F6C382EA4F5B6D3

FASTA26929,769
        10         20         30         40         50         60 
MSSKINFVKM HGLGNDFVII NKKDLTGTYD LSQLAKSMAK RHLGIGCDQF IIYEEQNDSY 

        70         80         90        100        110        120 
EMIIYNIDGS SAKLCGNATR CLAKLIYLDT GKKDITVVVG NKKLLCHVID ENNISVNVGG 

       130        140        150        160        170        180 
VSFNESWMPS RDKIWEFAER YMIDLKETIC VDVGNPHLVI FSKLELQDQK IVGEKLQDKA 

       190        200        210        220        230        240 
LFADGVNVNF AEVRDNKIYL SVWERGSGLT LACGSGACGS FAAGLKLGFI HSPCEVVFKH 

       250        260 
GSLIMKEENG NIIMQGPASL VAKGMYYCE 

« Hide

References

[1]"Complete genome sequencing of Rickettsia bellii."
Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU 85-389.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000849 Genomic DNA. Translation: ABV79201.1.
RefSeqYP_001496238.1. NC_009883.1.

3D structure databases

ProteinModelPortalA8GWH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391896.A1I_04280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV79201; ABV79201; A1I_04280.
GeneID5646811.
KEGGrbo:A1I_04280.
PATRIC17879660. VBIRicBel35792_0891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKDITVMV.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycRBEL391896:GH75-807-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_RICB8
AccessionPrimary (citable) accession number: A8GWH4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 45 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