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C5BUL6 (DAPF_TERTT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:TERTU_4180
OrganismTeredinibacter turnerae (strain ATCC 39867 / T7901) [Complete proteome] [HAMAP]
Taxonomic identifier377629 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadales genera incertae sedisTeredinibacter

Protein attributes

Sequence length276 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 – 276276Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000204068

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region210 – 2112Substrate binding By similarity
Region220 – 2212Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2191Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1591Substrate By similarity
Binding site1921Substrate By similarity
Site1611Important for catalytic activity By similarity
Site2101Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 219 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
C5BUL6 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: B0A1A3F29DD688F2

FASTA27629,913
        10         20         30         40         50         60 
MRLRFTKMHG LGNDFVMIDA ISQKVTITPE RARKLADRHF GVGCDQVLVV ESPDNPDADF 

        70         80         90        100        110        120 
RYRIFNNDGS EVENCGNGAR CFAVFVRQRQ LTAKSDIVVE TAAGLLRLHV LDDNQVTVNM 

       130        140        150        160        170        180 
GVPVLAPAQI PFVTPHEQPE YPLQLDNMEI TISAVSMGNP HAVTLVDNLA SFPVKTLGAQ 

       190        200        210        220        230        240 
IETHAQFPNR VNAGFMELIS RQEVKLRVFE RGVGETLACG TGACAAVVSG IVRGLLDTTV 

       250        260        270 
AVHLPGGSLS ITWEGAEKPV MMTGPAKAVF HGQVKL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001614 Genomic DNA. Translation: ACR12936.1.
RefSeqYP_003075443.1. NC_012997.1.

3D structure databases

ProteinModelPortalC5BUL6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING377629.TERTU_4180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR12936; ACR12936; TERTU_4180.
GeneID8214048.
KEGGttu:TERTU_4180.
PATRIC23875159. VBITerTur118718_3900.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycTTUR377629:GHSU-3791-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_TERTT
AccessionPrimary (citable) accession number: C5BUL6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 35 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