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A7Z8D3 (DAPF_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:RBAM_029280
OrganismBacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC 10A6 / FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

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_1000011835

Regions

Region11 – 122Substrate binding By similarity
Region76 – 783Substrate binding By similarity
Region217 – 2182Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2261Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site491Substrate By similarity
Binding site671Substrate By similarity
Binding site1661Substrate By similarity
Binding site1991Substrate By similarity
Site1681Important for catalytic activity By similarity
Site2171Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 226 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A7Z8D3 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: B88DC79712ED0C88

FASTA28430,917
        10         20         30         40         50         60 
MNSFRFTKMH GLGNSYIYVN QFEEQLPEER LAEIAVKVSS IHTGIGSDGM ILICPSEKAP 

        70         80         90        100        110        120 
VKMRIFNNDG SEGKNCGNGL RCVAKYAYEH KLTEETSFFI ETLSGLVKAD ITEDNGIVRE 

       130        140        150        160        170        180 
VAVDMGEPRL TKKELPMLGN EDERTIDETF VFGETELSGT AVSMGNPHIV FPVADINQAP 

       190        200        210        220        230        240 
LTTLGPVIEK DPRFPEGVNV EFVETVSADE LHFRVWERGS GITQACGTGA CAAAVASVLN 

       250        260        270        280 
GVSERNRDIT VHLAGGDLVI NWQDNGHVLM TGPAETVCSG VYYL 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 23117 / BGSC 10A6 / FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS75259.1.
RefSeqYP_001422490.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z8D3.
SMRA7Z8D3. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326423.RBAM_029280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS75259; ABS75259; RBAM_029280.
GeneID5461196.
KEGGbay:RBAM_029280.
PATRIC18751038. VBIBacAmy31356_2966.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAFMRIYNT.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycBAMY326423:GCM4-2926-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_BACA2
AccessionPrimary (citable) accession number: A7Z8D3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: April 16, 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