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B0SC36 (DAPF_LEPBA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. 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:LBF_0565
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]
Taxonomic identifier355278 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length280 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 – 280280Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000118673

Regions

Region10 – 112Substrate binding By similarity
Region73 – 753Substrate binding By similarity
Region215 – 2162Substrate binding By similarity
Region225 – 2262Substrate binding By similarity

Sites

Active site731Proton donor/acceptor By similarity
Active site2241Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site641Substrate By similarity
Binding site1641Substrate By similarity
Binding site1971Substrate By similarity
Site1661Important for catalytic activity By similarity
Site2151Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond73 ↔ 224 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B0SC36 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 05DE546E3D9C2CC6

FASTA28030,826
        10         20         30         40         50         60 
MKINFTKMEG IGNDYVYIDA TKNDIRLSPE QIQKLSDRNF GIGGDGVIFI RNSNSGEFQM 

        70         80         90        100        110        120 
DMYNSDGSSS EMCGNGVRCV GKFVYDHGLT KNQKPTIETG KGVLTLDLKT GTNGKVEMVT 

       130        140        150        160        170        180 
VDMGEPILKP SLVPIVWKGD EPVINQVIEV QGKQYHFTAV SMGNPHCVIY VDDADDFPVR 

       190        200        210        220        230        240 
EIGPIIENHP FFPRRVNVEF VSIKGKDHLY QRTWERGTGE TLACGTGACA VTVASILNGK 

       250        260        270        280 
TGRSVRIDLR GGTLHIEWQE NGSVFMTGPA KEVFSGEVEI 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / Ames.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000777 Genomic DNA. Translation: ABZ93101.1.
RefSeqYP_001961679.1. NC_010842.1.

3D structure databases

ProteinModelPortalB0SC36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355278.LBF_0565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ93101; ABZ93101; LBF_0565.
GeneID6388474.
KEGGlbf:LBF_0565.
PATRIC22340035. VBILepBif95142_0592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMANGLRCVI.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycLBIF355278:GHTJ-565-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_LEPBA
AccessionPrimary (citable) accession number: B0SC36
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 48 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