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B8D8F1 (DAPF_BUCA5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 38. 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:BUAP5A_582
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) [Complete proteome] [HAMAP]
Taxonomic identifier563178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length284 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 – 284284Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000124403

Regions

Region18 – 192Substrate binding By similarity
Region83 – 853Substrate binding By similarity
Region218 – 2192Substrate binding By similarity

Sites

Active site831Proton donor/acceptor By similarity
Active site2271Proton donor/acceptor By similarity
Binding site211Substrate By similarity
Binding site541Substrate By similarity
Binding site741Substrate By similarity
Binding site1671Substrate By similarity
Binding site2001Substrate By similarity
Site1691Important for catalytic activity By similarity
Site2181Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond83 ↔ 227 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B8D8F1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: C4AF9116AE63FE21

FASTA28431,995
        10         20         30         40         50         60 
MDSYYKNKKK INFSKMHGLK NDFMVINCIK KNVFLTSHII KKLSNRYTGI GFDQLLLVEK 

        70         80         90        100        110        120 
SNSLLTDFHY RIFNANGNEV EQCGNGARCF GLFLLLKGLT NKKKILISTK KKPLTIEFLT 

       130        140        150        160        170        180 
ENMIKVNMNE PDFKFYNLSS LQNVLDNNFS IKLINENLIC NLVSIGNPHC IIKVQSIKNA 

       190        200        210        220        230        240 
PVNIIGDNIE KNPIFPEGVN VSFMEILNKK HIKLRVYERN VGETKACGSA ACAAVAVGIA 

       250        260        270        280 
QKLLSDTVHV ELLGGKLIII WKGFGTPLYM VGPAKHVYDG YIYI 

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001161 Genomic DNA. Translation: ACL30927.1.
RefSeqYP_002468315.1. NC_011833.1.

3D structure databases

ProteinModelPortalB8D8F1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING107806.BU589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL30927; ACL30927; BUAP5A_582.
GeneID7262344.
KEGGbap:BUAP5A_582.
PATRIC21243435. VBIBucAph51993_0577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycBAPH563178:GHDF-582-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_BUCA5
AccessionPrimary (citable) accession number: B8D8F1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 38 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