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B8IZX7 (DAPF_DESDA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 30. 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:Ddes_1150
OrganismDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) [Complete proteome] [HAMAP]
Taxonomic identifier525146 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length287 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 – 287287Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000124410

Regions

Region12 – 132Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region221 – 2222Substrate binding By similarity
Region231 – 2322Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2301Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site481Substrate By similarity
Binding site661Substrate By similarity
Binding site1701Substrate By similarity
Binding site2031Substrate By similarity
Site1721Important for catalytic activity By similarity
Site2211Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 230 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B8IZX7 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 5540E21839668EF0

FASTA28731,239
        10         20         30         40         50         60 
MAVALRFTKM QGIGNDYVYI NGFQERIDSP GELARKISDR HFGIGSDGLV LILPSATADV 

        70         80         90        100        110        120 
RMRMFNADGS ESEMCGNAVR CVGKYVYDHG IQVKDVITVE TRAGVKIVRL LFEAGKVCGA 

       130        140        150        160        170        180 
TVDMGEPELH PARIPVLTET SGDGSQQRFV ARPVDVNGQL YEITAVSMGN PHAVIFMKGI 

       190        200        210        220        230        240 
DDLDLPRIGP RFEHHPLFPK RTNTEFAEVI SSTKVRMRVW ERGAGETLAC GTGACAVAVA 

       250        260        270        280 
CVLNGYAGRD VEVELKGGSL HIHWDEASNH VYMTGGAVTV FSGEYYI 

« Hide

References

[1]"Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Hazen T.C.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27774 / DSM 6949.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001358 Genomic DNA. Translation: ACL49054.1.
RefSeqYP_002479732.1. NC_011883.1.

3D structure databases

ProteinModelPortalB8IZX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING525146.Ddes_1150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL49054; ACL49054; Ddes_1150.
GeneID7284832.
KEGGdds:Ddes_1150.
PATRIC21735974. VBIDesDes50650_1348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycDDES525146:GIWF-1181-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_DESDA
AccessionPrimary (citable) accession number: B8IZX7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 30 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