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C4Z900 (DAPF_EUBR3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:EUBREC_1477
OrganismEubacterium rectale (strain ATCC 33656 / VPI 0990) [Complete proteome] [HAMAP]
Taxonomic identifier515619 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length285 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 – 285285Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000204060

Regions

Region71 – 733Substrate binding By similarity
Region218 – 2192Substrate binding By similarity
Region228 – 2292Substrate binding By similarity

Sites

Active site711Proton donor/acceptor By similarity
Active site2271Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site621Substrate By similarity
Binding site1671Substrate By similarity
Binding site2001Substrate By similarity
Site1691Important for catalytic activity By similarity
Site2181Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond71 ↔ 227 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
C4Z900 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 0C578469B0CE9E36

FASTA28531,778
        10         20         30         40         50         60 
MKFTKMHGCG NDYVYVNLFE EKLDDPARVS IYVSDRHFGI GSDGLITIGP SDKADFRMRI 

        70         80         90        100        110        120 
YNADGSEAEM CGNGIRCVAK YVYDHKLTDK TEISVETGAG IKYLTLYVEE NKVSQVRVDM 

       130        140        150        160        170        180 
GEPILTPGDI PVVKADGSAY SDDYRVIDEP ISAGNREWHM TCVSMGNPHA VVFVDDVAGF 

       190        200        210        220        230        240 
ELEKYGPLFE NHKMFPKRTN TEFVEILSRN EAKMRVWERG SAETWACGTG TCATVMACIL 

       250        260        270        280 
NKKTDNKVLV HLRGGDLTIE YIPETNHVFM TGPATEVFSG EIDII 

« Hide

References

[1]"Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla."
Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., Hettich R.L., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33656 / VPI 0990.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001107 Genomic DNA. Translation: ACR75231.1.
RefSeqYP_002937365.1. NC_012781.1.

3D structure databases

ProteinModelPortalC4Z900.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING515619.EUBREC_1477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR75231; ACR75231; EUBREC_1477.
GeneID7963842.
KEGGere:EUBREC_1477.
PATRIC21871185. VBIEubRec107985_1248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycEREC515619:GHMX-1471-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_EUBR3
AccessionPrimary (citable) accession number: C4Z900
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 33 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