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B7KQM2 (DAPF_METC4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:Mchl_2947
OrganismMethylobacterium extorquens (strain CM4 / NCIMB 13688) (Methylobacterium chloromethanicum) [Complete proteome] [HAMAP]
Taxonomic identifier440085 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length296 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 – 296296Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000124420

Regions

Region78 – 803Substrate binding By similarity
Region223 – 2242Substrate binding By similarity
Region233 – 2342Substrate binding By similarity

Sites

Active site781Proton donor/acceptor By similarity
Active site2321Proton donor/acceptor By similarity
Binding site171Substrate By similarity
Binding site491Substrate By similarity
Binding site691Substrate By similarity
Binding site1711Substrate By similarity
Binding site2051Substrate By similarity
Site1731Important for catalytic activity By similarity
Site2231Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond78 ↔ 232 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B7KQM2 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: F01A444D94EAD5F3

FASTA29631,877
        10         20         30         40         50         60 
MSPLANRRFL KMHGAGNAIV VLDLRGTAVR VTPAEARAIA ADVHSRFDQL MVVHDPVTPG 

        70         80         90        100        110        120 
TDAFMRIYNT DGSESGACGN GTRCVGYALL DDPAMARPAE NGALTLETKA GLVAVKRITE 

       130        140        150        160        170        180 
RSFTVDMGQP RLRWDEIPLT EPFLDTRRIE LQVGPIDDPI LHSPAAVSMG NPHAIFFVER 

       190        200        210        220        230        240 
DPDSYDLGRI GPLLEAHPIF PERANISIAE VTSRDTIKLR VWERGAGLTL ACGTAACATV 

       250        260        270        280        290 
VAASRLRMIG RAARVALPGG ELSIEWRADD HVLMTGPVYL EGEGTFSPDL FAGIDG 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium chloromethanicum CM4."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Marx C., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CM4 / NCIMB 13688.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001298 Genomic DNA. Translation: ACK83786.1.
RefSeqYP_002421714.1. NC_011757.1.

3D structure databases

ProteinModelPortalB7KQM2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING440085.Mchl_2947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK83786; ACK83786; Mchl_2947.
GeneID7115754.
KEGGmch:Mchl_2947.
PATRIC22500176. VBIMetChl132133_2915.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAFMRIYNT.
OrthoDBEOG6ND0M5.
ProtClustDBCLSK2331316.

Enzyme and pathway databases

BioCycMCHL440085:GCXT-3004-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_METC4
AccessionPrimary (citable) accession number: B7KQM2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 34 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