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Q6AE05 (DAPF_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Lxx15970
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length292 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 – 292292Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149846

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 site141Substrate By similarity
Binding site471Substrate By similarity
Binding site781Substrate By similarity
Binding site1641Substrate By similarity
Binding site1971Substrate By similarity
Site1661Important 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
Q6AE05 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 9A7944AB9769542C

FASTA29230,987
        10         20         30         40         50         60 
MATLHFTKGQ GTGNDFVLYA DPDGTLPLSA GQIAEICDRH FGVGADGVIR AVRSKRLPEG 

        70         80         90        100        110        120 
AEALADDEAA EWFMDYYNAD GSAAEMCGNG IRVYVRYLIE SRLVQLADGD TLPIGTRSGV 

       130        140        150        160        170        180 
RDVQRTLSGF QVDLGRWRLA GGEPLVRAKE LPVARLGLGI DLGNPHVVVA LADESELESA 

       190        200        210        220        230        240 
DLTYIPHLEP APQGGANVEF VVPHEPLVKD GVGRIRMRVH ERGSGETLSC GTGAAAAALA 

       250        260        270        280        290 
VRHWAGENAP GQWWVDVPGG TVGVRMFPTE DGEHVALSGP AELVYTGALE LA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT89391.1.
RefSeqYP_062496.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6AE05.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281090.Lxx15970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT89391; AAT89391; Lxx15970.
GeneID2938253.
KEGGlxx:Lxx15970.
PATRIC22336840. VBILeiXyl11655_1662.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMAGNPHTVV.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-1519-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_LEIXX
AccessionPrimary (citable) accession number: Q6AE05
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 59 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