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Q116P1 (DAPF_TRIEI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Tery_1173
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium

Protein attributes

Sequence length278 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 – 278278Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011978

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region213 – 2142Substrate binding By similarity
Region223 – 2242Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2221Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site471Substrate By similarity
Binding site661Substrate By similarity
Binding site1621Substrate By similarity
Binding site1951Substrate By similarity
Site1641Important for catalytic activity By similarity
Site2131Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 222 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q116P1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 77B39B893B94FCCA

FASTA27830,279
        10         20         30         40         50         60 
MTKSFTKYHG LGNDFILIDN RHQLQPILTP EQAIELCDRN FGIGADGVIF ALPGVKQTDY 

        70         80         90        100        110        120 
TMRIFNSDGS EPEMCGNGIR CLAKFIAELE NNNKTKYNIH TGAGIIVPEL QGDGQVTVDM 

       130        140        150        160        170        180 
GQPRLLASEI PTTLANADDK VVDQLLEVGG KSWFVTCVSM GNPHCITFVE DVTAIDLAKI 

       190        200        210        220        230        240 
GPKFEHNPVF PERTNTEFIQ VISPKYVKMR VWERGAGATL ACGTGACASV VAGVLTQNNE 

       250        260        270 
RLVTVELPGG CLEIEWSTID QKIYMTGPAE KVFTGIIA 

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000393 Genomic DNA. Translation: ABG50533.1.
RefSeqYP_721006.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ116P1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203124.Tery_1173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG50533; ABG50533; Tery_1173.
GeneID4244057.
KEGGter:Tery_1173.
PATRIC23986041. VBITriEry99848_1459.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycTERY203124:GJDR-1180-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_TRIEI
AccessionPrimary (citable) accession number: Q116P1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 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