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Q8Y5N9 (DAPF_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. 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:lmo2018
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length329 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
Reference 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 – 329329Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149851

Regions

Region82 – 843Substrate binding By similarity
Region224 – 2252Substrate binding By similarity
Region234 – 2352Substrate binding By similarity

Sites

Active site821Proton donor/acceptor By similarity
Active site2331Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site531Substrate By similarity
Binding site731Substrate By similarity
Binding site1701Substrate By similarity
Binding site2061Substrate By similarity
Site1721Important for catalytic activity By similarity
Site2241Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond82 ↔ 233 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q8Y5N9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9B5992BFDAEA83CD

FASTA32936,071
        10         20         30         40         50         60 
MATIHFTKVH GSQNDFFLVD EEGNQIMDWS DAKRADFAIK LCDREHSLGG ADGILYVTKS 

        70         80         90        100        110        120 
SEAGPIGQMR VVNSDGSIAS MCGNGLRTVA RYLLEKHALT EAKVETMKAI LDVKKATSLG 

       130        140        150        160        170        180 
FDIPTYQVEI SPVKFNAESL PMNVGVEKLF NQVVPELDAE LAFSAVSVPN PHLITFVDQT 

       190        200        210        220        230        240 
VLDSDRQETL ASYLNSENPY FPDGVNVSFV KRLSDDAIYV RTFERGVGFT NACGTAMSAC 

       250        260        270        280        290        300 
SLIKKMLDKD TFETPLNVYN DGGRVQVTAK KDEAGDISLQ LIGNATFVST GSVSYESDTV 

       310        320 
TELTNEATPE QAQYQELVKE VKEFLKTTE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591981 Genomic DNA. Translation: CAD00096.1.
PIRAB1327.
RefSeqNP_465542.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8Y5N9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo2018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD00096; CAD00096; CAD00096.
GeneID985823.
KEGGlmo:lmo2018.
PATRIC20313235. VBILisMon69206_2066.

Organism-specific databases

GenoListLMO2018.

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKDITVMV.
OrthoDBEOG6ND0M5.
PhylomeDBQ8Y5N9.

Enzyme and pathway databases

BioCycLMON169963:LMO2018-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_LISMO
AccessionPrimary (citable) accession number: Q8Y5N9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 69 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