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Q8F9V5 (DAPF_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:LA_0083
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length281 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 – 281281Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149848

Regions

Region11 – 122Substrate binding By similarity
Region74 – 763Substrate binding By similarity
Region216 – 2172Substrate binding By similarity
Region226 – 2272Substrate binding By similarity

Sites

Active site741Proton donor/acceptor By similarity
Active site2251Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site471Substrate By similarity
Binding site651Substrate By similarity
Binding site1651Substrate By similarity
Binding site1981Substrate By similarity
Site1671Important for catalytic activity By similarity
Site2161Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond74 ↔ 225 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q8F9V5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: DBECCC0E63DE1151

FASTA28130,966
        10         20         30         40         50         60 
MASLKFTKME GIGNDYVYID STRNDIRLTP EQIQKISDRN FGIGSDGVIF IRNSKQGDFM 

        70         80         90        100        110        120 
MDMYNSDGSS SEMCGNGIRC VAKYIYDHGL TSSKNPKIET GAGILEVDLK IGSGNKVDLV 

       130        140        150        160        170        180 
SVDMGKPVLV PSQIPVVWKN EETIIDQPLE IGDKNLKFTA VSMGNPHCVI FVDDSDEFPV 

       190        200        210        220        230        240 
RGIGPLIERH SIFPKRVNVE FVTIRGKDHL YQRTWERGAG ETLACGTGAC AVMVAGNLTR 

       250        260        270        280 
RSGKDVQIDL RGGTLRIQWQ ESGNILMTGP AREIFSGEIE I 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN47282.1.
RefSeqNP_710264.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F9V5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA0083.

Proteomic databases

PaxDbQ8F9V5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN47282; AAN47282; LA_0083.
GeneID1149426.
KEGGlil:LA_0083.
PATRIC22381009. VBILepInt91350_0089.

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycLINT189518:GJBB-73-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_LEPIN
AccessionPrimary (citable) accession number: Q8F9V5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 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