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Q5FQZ4 (DAPF_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:GOX1453
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length257 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 – 257257Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011882

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region193 – 1942Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2021Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1451Substrate By similarity
Binding site1751Substrate By similarity
Site1471Important for catalytic activity By similarity
Site1931Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 202 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q5FQZ4 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 787BB41D506C25B8

FASTA25727,293
        10         20         30         40         50         60 
MTLSFTKMHG LGNDFVVIDG RQNDPALETA TIRHLCDRRF GIGCDQLVLL TPPTLAGADV 

        70         80         90        100        110        120 
HVRFFNPDGS EAGACGNASR CVAKFVGGAP TLQTAAGLLP TAQDGDLFTV DMGTPRLDWQ 

       130        140        150        160        170        180 
DVPLSRACDT LHLPLHDAAA CSMGNPHATL FGDAFRAEAL GPGLERDPLF PERANIGFAQ 

       190        200        210        220        230        240 
ILSPIHMRLR VWERGAGLTL ACGSGACAAV VNAVRRGLTE RTCTVTMDGG DLRITWREDG 

       250 
HVFMTGPAVT VFHGTTA 

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000009 Genomic DNA. Translation: AAW61202.1.
RefSeqYP_191858.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FQZ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290633.GOX1453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW61202; AAW61202; GOX1453.
GeneID3249996.
KEGGgox:GOX1453.
PATRIC32610748. VBIGluOxy81109_1723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycGOXY290633:GHB3-1451-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_GLUOX
AccessionPrimary (citable) accession number: Q5FQZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 58 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