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Q47RR3 (DAPF_THEFY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:Tfu_0816
OrganismThermobifida fusca (strain YX) [Complete proteome] [HAMAP]
Taxonomic identifier269800 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length274 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 – 274274Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099270

Regions

Region85 – 873Substrate binding By similarity
Region207 – 2082Substrate binding By similarity
Region217 – 2182Substrate binding By similarity

Sites

Active site851Proton donor/acceptor By similarity
Active site2161Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site761Substrate By similarity
Binding site1571Substrate By similarity
Binding site1891Substrate By similarity
Site1591Important for catalytic activity By similarity
Site2071Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond85 ↔ 216 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q47RR3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 735D907C1084EECC

FASTA27428,547
        10         20         30         40         50         60 
MRFAKGHGTE NDFVILPDPD GELDLDAATV AALCDRRAGL GADGVLRVVR TKALDEPLTG 

        70         80         90        100        110        120 
EAATAQRCEW FMDYRNADGS VAEMCGNGVR VFARYLQEAG LVGAAAFEVG TRAGARHVVL 

       130        140        150        160        170        180 
EPDGNITVDM GPVRILGPGS ARLADGPVHG TRISVGNPHL ACRVARPVAE VDLSAPPLLR 

       190        200        210        220        230        240 
AEEFPQGANV EVFREVASGV LEMRVYERGA AETRSCGTGI VAAAAAATPP GEDARWTVRV 

       250        260        270 
PGGECTVVLE SGAARLSGPA VIVAEGDVRL SALR 

« Hide

References

[1]"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX."
Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N.
J. Bacteriol. 189:2477-2486(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000088 Genomic DNA. Translation: AAZ54854.1.
RefSeqYP_288877.1. NC_007333.1.

3D structure databases

ProteinModelPortalQ47RR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269800.Tfu_0816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ54854; AAZ54854; Tfu_0816.
GeneID3579695.
KEGGtfu:Tfu_0816.
PATRIC23902090. VBITheFus33945_0847.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycTFUS269800:GI42-832-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_THEFY
AccessionPrimary (citable) accession number: Q47RR3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 64 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