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B0TGR9 (DAPF_HELMI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Helmi_20550
ORF Names:HM1_2123
OrganismHeliobacterium modesticaldum (strain ATCC 51547 / Ice1) [Complete proteome] [HAMAP]
Taxonomic identifier498761 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacterium

Protein attributes

Sequence length281 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 – 281281Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099238

Regions

Region8 – 92Substrate binding By similarity
Region74 – 763Substrate binding By similarity
Region215 – 2162Substrate binding By similarity
Region225 – 2262Substrate binding By similarity

Sites

Active site741Proton donor/acceptor By similarity
Active site2241Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site471Substrate By similarity
Binding site651Substrate By similarity
Binding site1641Substrate By similarity
Binding site1971Substrate By similarity
Site1661Important for catalytic activity By similarity
Site2151Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond74 ↔ 224 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B0TGR9 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 6412759EBF2E3EEE

FASTA28130,627
        10         20         30         40         50         60 
MEFVKMHGLG NDFIVVNAME PPLLDREDWE EIAVRICDRH YGIGGDGLIL LFPSDKADIR 

        70         80         90        100        110        120 
WRILNSDGSE PEMCGNGIRC LARYVYERGI VAKRRIEVET LAGIIVPEII TDAAGAVTGV 

       130        140        150        160        170        180 
CVDMGEPRLQ RHQIPMVGPE GPAVNQELVV GDAVVRVTAL SMGNPHCLIY VNDIDEAPVT 

       190        200        210        220        230        240 
TLGPKVEVHP AFPAKTNVEF VQVVAPDEVQ MRVWERGAGP TLACGTGACA TVVGSVLNGY 

       250        260        270        280 
TDRKVTVHLA GGPLHIEWRE ENNRVYMTGP AVEVFRGELP L 

« Hide

References

[1]"The genome of Heliobacterium modesticaldum, a phototrophic representative of the Firmicutes containing the simplest photosynthetic apparatus."
Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.
J. Bacteriol. 190:4687-4696(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51547 / Ice1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000930 Genomic DNA. Translation: ABZ84680.1.
RefSeqYP_001680691.1. NC_010337.2.

3D structure databases

ProteinModelPortalB0TGR9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498761.HM1_2123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ84680; ABZ84680; HM1_2123.
GeneID5909192.
KEGGhmo:HM1_2123.
PATRIC22108313. VBIHelMod36755_1917.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAFMRIYNT.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycHMOD498761:GI46-2115-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_HELMI
AccessionPrimary (citable) accession number: B0TGR9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 44 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