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Q8AAB7 (DAPF_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:BT_0548
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length267 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
Reference 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 – 267267Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149821

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
Q8AAB7 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: 7BE62A3C36B3A3FF

FASTA26728,970
        10         20         30         40         50         60 
MTTKIKFTKM HGAGNDYIYV DTTRYPIAAP EKKAIEWSKF HTGIGSDGLI LIGSSDKADF 

        70         80         90        100        110        120 
SMRIFNADGS EAMMCGNGSR CVGKYVYEYG LTAKKEITLD TRSGIKVLKL HVEGGKVTAV 

       130        140        150        160        170        180 
TVDMGSPLET EAVDFGDQFP FQSTRVSMGN PHLVTFVEDI TQINLPEIGP QLENYHLFPD 

       190        200        210        220        230        240 
RTNVEFAQIV GKDTIRMRVW ERGSGITQAC GTGACATAVA AVLHGLAGRK CDIIMDGGTV 

       250        260 
TIEWEEATGH ILMTGPATKV FDGEMEG 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO75655.1.
RefSeqNP_809461.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8AAB7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_0548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO75655; AAO75655; BT_0548.
GeneID1072044.
KEGGbth:BT_0548.
PATRIC21055843. VBIBacThe70966_0548.

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-550-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 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_BACTN
AccessionPrimary (citable) accession number: Q8AAB7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: February 19, 2014
This is version 69 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