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Q64SY7 (DAPF_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:BF2642
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

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_1000011841

Regions

Region75 – 773Substrate binding By similarity
Region201 – 2022Substrate binding By similarity
Region211 – 2122Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2101Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site481Substrate By similarity
Binding site661Substrate By similarity
Binding site1501Substrate By similarity
Binding site1831Substrate By similarity
Site1521Important for catalytic activity By similarity
Site2011Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 210 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q64SY7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: DBE82CC62E974EE9

FASTA26929,368
        10         20         30         40         50         60 
MARAIQFTKM HGTGNDYIYV NTLRFPIARP EKAAIEWSAY HTGIGSDGLV LIGHSDKADF 

        70         80         90        100        110        120 
SMRIFNADGS EAMMCGNASR CIGKYLYEYG LTSKNVITLD TLSGIKILEL HLEGRTVETV 

       130        140        150        160        170        180 
TVDMGVPLET DTIDFDGEFP FLSTQVSMGN PHLVTFVDDI RIVNLSEMGP KLEKHPLFPD 

       190        200        210        220        230        240 
RTNVEFAQIT GENTIRMRVW ERGSGITQAC GTGACATAVA AHLTGRTGRT VNVVMDGGTL 

       250        260 
TIEWDEATGH ISMTGPAVKV FDGTIELRE 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD49392.1.
RefSeqYP_099926.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64SY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295405.BF2642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD49392; BAD49392; BF2642.
GeneID3083667.
KEGGbfr:BF2642.
PATRIC21050915. VBIBacFra17906_2554.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000073580.
KOK01778.
OMAVFDRYFL.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

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_BACFR
AccessionPrimary (citable) accession number: Q64SY7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: June 11, 2014
This is version 62 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