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Q9PJW2 (DAPF_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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:TC_0714
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length269 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 – 269269Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149830

Regions

Region72 – 743Substrate binding By similarity
Region197 – 1982Substrate binding By similarity
Region208 – 2092Substrate binding By similarity

Sites

Active site721Proton donor/acceptor By similarity
Active site2071Proton donor/acceptor By similarity
Binding site201Substrate By similarity
Binding site451Substrate By similarity
Binding site631Substrate By similarity
Binding site1791Substrate By similarity
Site1471Important for catalytic activity By similarity
Site1971Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond72 ↔ 207 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q9PJW2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: ECDE5D168060E1C2

FASTA26929,864
        10         20         30         40         50         60 
MGSFSPLMTY RYHLYSGTGN SFILGEFIPP LQHIVFLCQK EKVDGFLCVE PSEIADAKLT 

        70         80         90        100        110        120 
IFNSDGSEAS MCGNGLRCVM AHVAQSLGLE DVSIETVRGV YQGKFFSMDR VLVDMTLLDW 

       130        140        150        160        170        180 
KKTKKTLTHV LPGMPEEVFF IDTGVPHVVV FVPDVNKVPV QEWGAFLRYH EDFRPNGVNV 

       190        200        210        220        230        240 
DFVQTKKEDT LLVYTYERGC ERETLSCGTG MLASALVAAD VFSLEQDFSL LVCSRSGNIV 

       250        260 
KIFSENGKVF LEGPVTLLNC SENIGEFAP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF73596.1.
RefSeqNP_297088.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PJW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF73596; AAF73596; TC_0714.
GeneID1246077.
KEGGcmu:TC_0714.
PATRIC20372894. VBIChlMur19118_0757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMANGLRCVI.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-739-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_CHLMU
AccessionPrimary (citable) accession number: Q9PJW2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 79 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