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Q73W21 (DAPF_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:MAP_2840c
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length294 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 – 294294Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011908

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
Q73W21 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: DFBB58E0EB873277

FASTA29429,958
        10         20         30         40         50         60 
MKFAKGHGTE NDFVLLCDPP AELRLTGAGV AALCDRRRGL GADGVLRVTA AAAAAAAGVL 

        70         80         90        100        110        120 
DRLPDGVAGD DWYMDYRNAD GSVAQMCGNG VRVFAHYLRA SGLETRDEFV VGSLAGPRPV 

       130        140        150        160        170        180 
TVHAADATGA DVSVDMGKAN TLGGGGEAFE ATVGGRRFAG LAVDVGNPHL ACLDPELSVD 

       190        200        210        220        230        240 
ELAALDVAAP VSFDAAQFPD GVNIEVLTAP AAGVVHMRVH ERGVGETRSC GTGTVAAVVA 

       250        260        270        280        290 
ALAAAGADTG TLTVRVPGGD VVVTVTDATS YLRGPSVLVA HGEISEEWWQ QAQR 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS05157.1.
RefSeqNP_961774.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73W21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP2840c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS05157; AAS05157; MAP_2840c.
GeneID2717509.
KEGGmpa:MAP2840c.
PATRIC17998398. VBIMycAvi108102_3009.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-2880-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_MYCPA
AccessionPrimary (citable) accession number: Q73W21
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 63 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