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B6YS11 (DAPF_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 38. 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:CFPG_720
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesCandidatus Azobacteroides

Protein attributes

Sequence length275 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 – 275275Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000124398

Regions

Region71 – 733Substrate binding By similarity
Region211 – 2122Substrate binding By similarity
Region221 – 2222Substrate binding By similarity

Sites

Active site711Proton donor/acceptor By similarity
Active site2201Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site621Substrate By similarity
Binding site1601Substrate By similarity
Binding site1931Substrate By similarity
Site1621Important for catalytic activity By similarity
Site2111Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond71 ↔ 220 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B6YS11 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: E6E7FF4BEA1D0FD5

FASTA27531,002
        10         20         30         40         50         60 
MKFTKMHGAG NDYIYIDCFK EKIDCPEELA IRLSDRHKGI GSDGLVLIMP SDKCSFRMRM 

        70         80         90        100        110        120 
FNSDGSEAQM CGNAIRCVGK YVYDNGYTRK LNITIETLAG VKQLELFPTN DKIRKVKVNM 

       130        140        150        160        170        180 
GKPILLAKDI PVIWEKEKLI YETIDFSSEQ WILTAVSMGN PHVVIFVEKV SRLDVKRIGK 

       190        200        210        220        230        240 
EIEHHPMFPE KINVDFVEIL SLYHAKMRVW ERGSGETQAC GTGACAALVA SVLNGKLNRK 

       250        260        270 
ATISLLGGDL ELEWDEKTEH VFMTGDASLV FIGEF 

« Hide

References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010656 Genomic DNA. Translation: BAG83983.1.
RefSeqYP_002309394.1. NC_011565.1.

3D structure databases

ProteinModelPortalB6YS11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511995.CFPG_720.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG83983; BAG83983; CFPG_720.
GeneID7040025.
KEGGaps:CFPG_720.
PATRIC31963476. VBICanAzo57536_1091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAINTGSPH.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycCAZO511995:GKF1-758-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_AZOPC
AccessionPrimary (citable) accession number: B6YS11
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 20, 2009
Last modified: June 11, 2014
This is version 38 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