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Q1LTX0 (DAPF_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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:BCI_0125
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

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_1000058538

Regions

Region8 – 92Substrate binding By similarity
Region73 – 753Substrate binding By similarity
Region208 – 2092Substrate binding By similarity

Sites

Active site731Proton donor/acceptor By similarity
Active site2171Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site441Substrate By similarity
Binding site641Substrate By similarity
Binding site1571Substrate By similarity
Binding site1901Substrate By similarity
Site1591Important for catalytic activity By similarity
Site2081Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond73 ↔ 217 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q1LTX0 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 60E2349CB8D80347

FASTA27430,702
        10         20         30         40         50         60 
MQFSKMHGLG NDFMVVDVVT QNVYLSPTKI RFLANRHSGV GFDQLLFVEP PYDPEIDFHY 

        70         80         90        100        110        120 
RIFNADGSEV TQCGNGARCL AHFVRMKKLT NKREIYISTQ TSRMVLTIIE NNMVRVNMGV 

       130        140        150        160        170        180 
PKFELPQIPF DMHQIEKKEI LYLAKNYIFG GIVSIGNPHC IMIVNNVDSA QVSIIGPILE 

       190        200        210        220        230        240 
IHKYFSERTN VGFMQVINRE QVLLRVYERG VGETQACGSG ACAAVAIGIR LGLLAEQVQV 

       250        260        270 
ALPGGKLVIY WRGPGQSLYM TGPAVHIYDG FIND 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14159.1.
RefSeqYP_588594.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTX0.
SMRQ1LTX0. Positions 1-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374463.BCI_0125.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF14159; ABF14159; BCI_0125.
GeneID4056212.
KEGGbci:BCI_0125.
PATRIC21073749. VBIBauCic75062_0125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycBCIC374463:GI6Q-125-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_BAUCH
AccessionPrimary (citable) accession number: Q1LTX0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 30, 2006
Last modified: June 11, 2014
This is version 57 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