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A6WXE4 (DAPF_OCHA4) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 46. 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:Oant_0927
OrganismOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [Complete proteome] [HAMAP]
Taxonomic identifier439375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Protein attributes

Sequence length300 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 – 300300Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011921

Regions

Region12 – 132Substrate binding By similarity
Region76 – 783Substrate binding By similarity
Region215 – 2162Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2241Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site471Substrate By similarity
Binding site671Substrate By similarity
Binding site1631Substrate By similarity
Binding site1971Substrate By similarity
Site1651Important for catalytic activity By similarity
Site2151Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 224 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A6WXE4 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 2E69921F44F5152F

FASTA30032,658
        10         20         30         40         50         60 
MATKAAFAKM NGLGNQIIVA DMRGRADRIT PEAAIRLAGD SETAFDQIMA IHDPRTAGTD 

        70         80         90        100        110        120 
NYIAIINCDG TEAQACGNGT RCVVQALAAE TGRQAFTFET RAGILTATEH EDGLISVDMG 

       130        140        150        160        170        180 
KPRFDWQDIP LAEEFRDTRM IELQVGPIDA PVLHSPSVAS MGNPHAIFWV DRDVWSYELE 

       190        200        210        220        230        240 
KFGPLLEHHP IFPERANISI AHVTSPETID LRTWERGAGL TRACGSAACA AAVSAVRTRR 

       250        260        270        280        290        300 
TGRTVTVNVP GGPLRIEWRD DDHVMMTGPA EWEFSGTFDP ATGEWSRDAQ NDKPTDRGAA 

« Hide

References

[1]"Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts."
Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.
J. Bacteriol. 193:4274-4275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000758 Genomic DNA. Translation: ABS13648.1.
RefSeqYP_001369477.1. NC_009667.1.

3D structure databases

ProteinModelPortalA6WXE4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439375.Oant_0927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS13648; ABS13648; Oant_0927.
GeneID5378631.
KEGGoan:Oant_0927.
PATRIC20466899. VBIOchAnt73124_0972.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycOANT439375:GJIT-935-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_OCHA4
AccessionPrimary (citable) accession number: A6WXE4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: June 11, 2014
This is version 46 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