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Q46185 (DAPF_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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:CPE1846
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length272 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.

Sequence caution

The sequence CAA60229.1 differs from that shown. Reason: Frameshift at position 181.

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 – 272272Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149835

Regions

Region72 – 743Substrate binding By similarity
Region208 – 2092Substrate binding By similarity
Region218 – 2192Substrate binding By similarity

Sites

Active site721Proton donor/acceptor By similarity
Active site2171Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site451Substrate By similarity
Binding site631Substrate By similarity
Binding site1901Substrate By similarity
Site1621Important for catalytic activity By similarity
Site2081Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond72 ↔ 217 HAMAP-Rule MF_00197

Experimental info

Sequence conflict1831E → D Ref.2
Sequence conflict1931F → S in CAA60229. Ref.2
Sequence conflict2011T → P in CAA60229. Ref.2
Sequence conflict2061T → P in CAA60229. Ref.2
Sequence conflict2301K → N in CAA60229. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q46185 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: 60DB1A8527815C05

FASTA27230,084
        10         20         30         40         50         60 
MKFSKMHGNG NDFIVIEDLN NEYLGKEGEI AQKMCHRRFG IGADGILIVR KNENCDIEMV 

        70         80         90        100        110        120 
IINSDGSYAA MCGNGIRCFA KYVYEKGIVK KDVLDVLTGD GVKRIFLEIE NDKVKTINVN 

       130        140        150        160        170        180 
MGFGDFKPKN IPALCDEEII EKKVSVGNGN FEITSLLMGV PHTIIFEEEK YPIECGRDIE 

       190        200        210        220        230        240 
KYELFPQGTN VNFCKVIDRN TMEVRTWERG AGPTLACGTG NCASVIAANK LGLVDKEVKV 

       250        260        270 
IVPGGELKVN IEDDGVKMIG NASFICDGTY LF 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.
[2]"Rapid expansion of the physical and genetic map of the chromosome of Clostridium perfringens CPN50."
Katayama S., Dupuy B., Garnier T., Cole S.T.
J. Bacteriol. 177:5680-5685(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-238.
Strain: CPN50.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB81552.1.
X86511 Genomic DNA. Translation: CAA60229.1. Frameshift.
RefSeqNP_562762.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ46185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE1846.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB81552; BAB81552; BAB81552.
GeneID990155.
KEGGcpe:CPE1846.
PATRIC19497647. VBICloPer59675_1919.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycCPER195102:GJFM-1894-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_CLOPE
AccessionPrimary (citable) accession number: Q46185
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 31, 2002
Last modified: June 11, 2014
This is version 94 of the entry and version 2 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