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Q5N013 (DAPF_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:syc2167_c
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length280 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 – 280280Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011976

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
Q5N013 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 028A3310F9437BAC

FASTA28029,971
        10         20         30         40         50         60 
MSLQFAKYHG LGNDFILVDN RESGEPRLTP EQAVQVCDRN FGVGADGVIF ALPGSGDSDY 

        70         80         90        100        110        120 
VMRIFNSDGS EPEMCGNGIR CLAKFLSELD GGAQSRYRIA TGAGLIVPTL TETGLVTVDM 

       130        140        150        160        170        180 
GPAYLKPVEI PTTLTGTGDR VVEADLEVGD RPWKVTTVSM GNPHCITFVE DVAAVPLAEI 

       190        200        210        220        230        240 
GPLFEHHPVF PQRTNTEFVE VVRPDYLKMR VWERGAGATL ACGTGACATL VAAVLTGRSD 

       250        260        270        280 
RQATVELPGG PLQIEWREDG HLFMTGPAVK VFSGSMELAA 

« Hide

References

[1]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008231 Genomic DNA. Translation: BAD80357.1.
RefSeqYP_172877.1. NC_006576.1.

3D structure databases

ProteinModelPortalQ5N013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc2167_c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD80357; BAD80357; syc2167_c.
GeneID3200209.
KEGGsyc:syc2167_c.
PATRIC32490478. VBISynElo117686_2469.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-2223-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_SYNP6
AccessionPrimary (citable) accession number: Q5N013
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 60 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