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Q81XR2 (DAPF_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BA_5170, GBAA_5170, BAS4806
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length288 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

Subunit structure

Homodimer. Ref.4

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 term3D-structure
Complete proteome
Reference 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 – 288288Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011837

Regions

Region11 – 122Substrate By similarity
Region76 – 783Substrate binding By similarity
Region217 – 2182Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2261Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site671Substrate By similarity
Binding site1661Substrate By similarity
Binding site1991Substrate By similarity
Site1681Important for catalytic activity Potential
Site2171Important for catalytic activity Potential

Amino acid modifications

Disulfide bond76 ↔ 226 By similarity

Secondary structure

................................................ 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q81XR2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F82364D2AC4202CA

FASTA28831,613
        10         20         30         40         50         60 
MSQFSFTKMH GLGNSYIYVN MFEEQIPEED LALVAEKVSN INTGIGADGM ILICPSDVAP 

        70         80         90        100        110        120 
VKMRMFNNDG SEGKSCGNGL RCVAKYAYEH KLVEDTVFTI ETLAGIVTAE VTVEEGKVTL 

       130        140        150        160        170        180 
AKIDMGAPRL TRAEIPMLGE GETPFIRENF LYNNHRYAFT AVSMGNPHAV IFVDDVEQAP 

       190        200        210        220        230        240 
LTTLGPVLET HEMFPERVNV EFIEILNEEE MNFRVWERGS GVTQACGTGA CAAVVASILN 

       250        260        270        280 
GKMERGKEIT VHLAGGDLMI AWTEEGNVLM KGPAEVICRG VYEYKIEA 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[4]"Crystal structure of the catalytically active form of diamin epimerase from Bacillus anthracis."
Matho M.H., Fukuda K., Santelli E., Jaroszewski L., Liddington R.C., Roper D.
Submitted (FEB-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28840.1.
AE017225 Genomic DNA. Translation: AAT57099.1.
AE017334 Genomic DNA. Translation: AAT70160.1.
RefSeqNP_847354.1. NC_003997.3.
YP_031049.1. NC_005945.1.
YP_052652.1. NC_007530.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OTNX-ray2.40A/B1-288[»]
ProteinModelPortalQ81XR2.
SMRQ81XR2. Positions 1-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ81XR2. 3 interactions.
STRING198094.BA_5170.

Protocols and materials databases

DNASU1084119.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP28840; AAP28840; BA_5170.
AAT57099; AAT57099; BAS4806.
AAT70160; AAT70160; GBAA_5170.
GeneID1084119.
2821103.
2848459.
KEGGban:BA_5170.
bar:GBAA_5170.
bat:BAS4806.

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycANTHRA:DAPF-MONOMER.
BANT260799:GJAJ-4884-MONOMER.
BANT261594:GJ7F-5046-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...

Other

EvolutionaryTraceQ81XR2.

Entry information

Entry nameDAPF_BACAN
AccessionPrimary (citable) accession number: Q81XR2
Secondary accession number(s): Q6F086, Q6HRI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways