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A3PYF9 (DAPF_MYCSJ) 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:Mjls_2150
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length293 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 – 293293Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011910

Regions

Region87 – 893Substrate binding By similarity
Region220 – 2212Substrate binding By similarity
Region230 – 2312Substrate binding By similarity

Sites

Active site871Proton donor/acceptor By similarity
Active site2291Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site781Substrate By similarity
Binding site1661Substrate By similarity
Binding site2021Substrate By similarity
Site1681Important for catalytic activity By similarity
Site2201Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond87 ↔ 229 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A3PYF9 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 25A9C82578F1765A

FASTA29330,530
        10         20         30         40         50         60 
MQFAKGHGTQ NDFVLLPDLD ARLALTPAVV SALCDRRRGL GADGVLRVTT AKAALSAGVF 

        70         80         90        100        110        120 
ERLPEGVGAG DWYMDYRNAD GSIAQMCGNG VRVFAHYLRA ADLESRDEFV VGSLAGPRPV 

       130        140        150        160        170        180 
VLHGFDLAHR SRAEVTVEMG KVNLLGSGSA VVGGRRFTGL GIDVGNPHLA CVDTTLTEAE 

       190        200        210        220        230        240 
LAALDVAAPV DFDPAQFPDG VNVEVLTALR DGAVSMRVHE RGVGETRSCG TGTVAAAVAA 

       250        260        270        280        290 
LAQEGAAVGT LDVRIPGGVV TVSVTDTTSF LRGPSELVAT GELAGEWWQS HQR 

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000580 Genomic DNA. Translation: ABN97936.1.
RefSeqYP_001070427.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3PYF9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164757.Mjls_2150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN97936; ABN97936; Mjls_2150.
GeneID4877870.
KEGGmjl:Mjls_2150.
PATRIC18090428. VBIMycSp51234_2154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycMSP164757:GHV3-2161-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_MYCSJ
AccessionPrimary (citable) accession number: A3PYF9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 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