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A0PT80 (DAPF_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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:MUL_3369
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length290 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 – 290290Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011913

Regions

Region87 – 893Substrate binding By similarity
Region217 – 2182Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site871Proton donor/acceptor By similarity
Active site2261Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site781Substrate By similarity
Binding site1631Substrate By similarity
Binding site1991Substrate By similarity
Site1651Important for catalytic activity By similarity
Site2171Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond87 ↔ 226 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A0PT80 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 48269BB5129D8719

FASTA29030,071
        10         20         30         40         50         60 
MIFAKGHGTQ NDFVLLPDVA ARLSLTAAQV AALCDRRRGL GADGILRVTT ADAAVAAGVL 

        70         80         90        100        110        120 
HRLPDGVSPG DWYMDYRNAD GSTAQMCGNG VRVFAHYLRA SGLETRDEFV VGSLAGPRPV 

       130        140        150        160        170        180 
TVHHADQTHA DVTVDMGKAN KLGPGEAVVG GRRLSGVAVD VGNPHLACLD PGLTPEQLAA 

       190        200        210        220        230        240 
LDVGAPVSFD HAQFPEGVNV EVLTARAAGV VCMRVHERGV GETRSCGTGT VAAAVAALAS 

       250        260        270        280        290 
AGQETGTLTV RIPGGDVTVN ITDATSLLRG PSVLVASGEI SEEWWRDQRR 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL05549.1.
RefSeqYP_907020.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PT80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_3369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL05549; ABL05549; MUL_3369.
GeneID4553492.
KEGGmul:MUL_3369.
PATRIC18174189. VBIMycUlc37413_3922.

Organism-specific databases

GenoListMUL_3369.
CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

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. 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_MYCUA
AccessionPrimary (citable) accession number: A0PT80
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: June 11, 2014
This is version 52 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