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B0C312 (DAPF_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 45. 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:AM1_2349
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris

Protein attributes

Sequence length283 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 – 283283Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000077687

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region216 – 2172Substrate binding By similarity
Region226 – 2272Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2251Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site471Substrate By similarity
Binding site661Substrate By similarity
Binding site1651Substrate By similarity
Binding site1981Substrate By similarity
Site1671Important for catalytic activity By similarity
Site2161Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 225 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B0C312 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 33E9B96A9A211B28

FASTA28330,692
        10         20         30         40         50         60 
MRVEFTKYQG LGNDFILIDN RHQAQPCLTP DQAVQMCDRN FGIGGDGVIF ALPPEGDTDY 

        70         80         90        100        110        120 
TMRIYNSDGS EPEMCGNGIR CLARFLAHLE GKPLQTDITY RIHTLAGTIT PSLQADGLVK 

       130        140        150        160        170        180 
VDMGPPFLVP QEIPTTLGEG TDPVVNQPLE VAGQSWPVTC VSMGNPHCIT FVDDLEAIDF 

       190        200        210        220        230        240 
QTLGPQFEHH PVFPQRINTE FIQVIRPDYL KMLVWERGAG PTLACGTGAC AVLVAGVLTG 

       250        260        270        280 
KSQSQATIEL PGGPLQIRWA GEGQSVFMTG PAEKVFTGIY ETG 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW27359.1.
RefSeqYP_001516673.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING329726.AM1_2349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW27359; ABW27359; AM1_2349.
GeneID5681162.
KEGGamr:AM1_2349.
PATRIC20619022. VBIAcaMar40141_2144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-2338-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...

Entry information

Entry nameDAPF_ACAM1
AccessionPrimary (citable) accession number: B0C312
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: June 11, 2014
This is version 45 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