Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B0RHB0 (DAPF_CLAMS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:CMS1212
OrganismClavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum) [Complete proteome] [HAMAP]
Taxonomic identifier31964 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length292 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 – 292292Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000077694

Regions

Region87 – 893Substrate binding By similarity
Region221 – 2222Substrate binding By similarity
Region231 – 2322Substrate binding By similarity

Sites

Active site871Proton donor/acceptor By similarity
Active site2301Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site781Substrate By similarity
Binding site1641Substrate By similarity
Binding site1971Substrate By similarity
Site1661Important for catalytic activity By similarity
Site2211Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond87 ↔ 230 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B0RHB0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 9AC0AEF004FE3313

FASTA29230,562
        10         20         30         40         50         60 
MADLQFTKGQ GTGNDFVLFA DPAGEIDLTD TQVQALCDRH FGIGADGTIR AVLSSRIPEG 

        70         80         90        100        110        120 
RAALDEDPDA EWFMDYRNVD GSPAEMCGNG IRVFTLFLIE NGLIELPPGR TVPIGTRAGV 

       130        140        150        160        170        180 
RDVQRSGSGF QVDLGRWALA GGEPLVRAKD LQVARPGLGI DVGNPHVVVA LSSEDELAEA 

       190        200        210        220        230        240 
DLAFAPQLDP EPAEGANVEL VVPADPLIVD GVGHITMRVH ERGSGETLSC GTGAAAAALA 

       250        260        270        280        290 
IRHWAGAAAP HQWRVQLPGG VLGVRMFPTE DGEHVGLSGP AELVFDGVVA LA 

« Hide

References

[1]"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation."
Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A.
J. Bacteriol. 190:2150-2160(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM849034 Genomic DNA. Translation: CAQ01327.1.
RefSeqYP_001709949.1. NC_010407.1.

3D structure databases

ProteinModelPortalB0RHB0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING31964.CMS_1212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ01327; CAQ01327; CMS1212.
GeneID6157094.
KEGGcms:CMS_1212.
PATRIC21459422. VBIClaMic4666_1273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMAGNPHTVV.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycCMIC31964:GJBN-1220-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_CLAMS
AccessionPrimary (citable) accession number: B0RHB0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 42 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