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P46814 (DAPF_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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:ML0996
ORF Names:B2235_C3_233
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length296 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 – 296296Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149852

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 site111Substrate By similarity
Binding site441Substrate By similarity
Binding site781Substrate By similarity
Binding site1671Substrate By similarity
Binding site2031Substrate By similarity
Site1691Important 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
P46814 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F0FBD68A0D5BAF5C

FASTA29630,640
        10         20         30         40         50         60 
MIFAKGHGTQ NDFVVLPDVE ADVTFTAAQV AALCNRRQGL GADGVLRVTT AGAAVTAGVL 

        70         80         90        100        110        120 
EHLPDGVSCS DWYMDYRNAD GSVAQMCGNG VRVFAHYLRA SGLESCDEFV VGSLAGPRLV 

       130        140        150        160        170        180 
NVHHVDELNA DVTVDMGKAN LLGSGGPAFA VTVGGRRFSG VAVDVGNPHL ACMDPQLSLE 

       190        200        210        220        230        240 
ELAALDLGAP VHLDRVQFPD GVNIEVLTAP VDGMVQMRVH ERGVGETRSC GTGTVAAAVA 

       250        260        270        280        290 
ALASAGADTG TLTVRVPGGD VVITITDVTS YLRGPSVLVA HGELADAWWY SLARSC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00019 Genomic DNA. Translation: AAA17279.1.
AL583920 Genomic DNA. Translation: CAC31377.1.
PIRS72943.
RefSeqNP_301738.1. NC_002677.1.

3D structure databases

ProteinModelPortalP46814.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML0996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31377; CAC31377; CAC31377.
GeneID910020.
KEGGmle:ML0996.
PATRIC18053718. VBIMycLep78757_1804.

Organism-specific databases

LepromaML0996.
CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

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_MYCLE
AccessionPrimary (citable) accession number: P46814
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 84 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