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C1A8U3 (DAPF_GEMAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 31. 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:GAU_1611
OrganismGemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC 100505) [Complete proteome] [HAMAP]
Taxonomic identifier379066 [NCBI]
Taxonomic lineageBacteriaGemmatimonadetesGemmatimonadalesGemmatimonadaceaeGemmatimonas

Protein attributes

Sequence length277 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 – 277277Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000204061

Regions

Region74 – 763Substrate binding By similarity
Region198 – 1992Substrate binding By similarity
Region209 – 2102Substrate binding By similarity

Sites

Active site741Proton donor/acceptor By similarity
Active site2081Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site461Substrate By similarity
Binding site651Substrate By similarity
Binding site1801Substrate By similarity
Site1481Important for catalytic activity By similarity
Site1981Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond74 ↔ 208 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
C1A8U3 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 729354861C6A19DF

FASTA27728,993
        10         20         30         40         50         60 
MSFVKMTGSG NDFVFFDGRT TPIDLVTQPE AIKAICNRYN GIGADGLVVL EPLQEEADVR 

        70         80         90        100        110        120 
VHYYNSDGTA ADLCGNATLC STAISAQWGI TSASGMRLAT GAGLINSRID GLPAIALQPI 

       130        140        150        160        170        180 
TDIRPDMPIA PATAQGRRVG FAVAGIPHLV ILCEDADAVD VAGAGPALRR HEATGPAGAN 

       190        200        210        220        230        240 
VNWVSPRPDG SWRYRTFERG VEGETLACGT GAVATAVLLR SWGLSDGATT TIRTSSGRDV 

       250        260        270 
EVDLEPLTAP DGRSLEGFRP TLRGEGRVVF RGEIAGL 

« Hide

References

[1]"Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a novel phylum Gemmatimonadetes."
Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T-27 / DSM 14586 / JCM 11422 / NBRC 100505.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009153 Genomic DNA. Translation: BAH38653.1.
RefSeqYP_002761123.1. NC_012489.1.

3D structure databases

ProteinModelPortalC1A8U3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379066.GAU_1611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH38653; BAH38653; GAU_1611.
GeneID7704781.
KEGGgau:GAU_1611.
PATRIC21956116. VBIGemAur55831_1657.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycGAUR379066:GI3W-1640-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689. PTHR31689. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPF_GEMAT
AccessionPrimary (citable) accession number: C1A8U3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 31 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