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A1AWJ5 (DAPF_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Rmag_0550
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length271 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 – 271271Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011956

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region206 – 2072Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2151Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1551Substrate By similarity
Binding site1881Substrate By similarity
Site1571Important for catalytic activity By similarity
Site2061Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 215 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A1AWJ5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: C2F605B4314CBAEE

FASTA27129,578
        10         20         30         40         50         60 
MLINFVKMHG LGNDFMMVDN LAGDITFNAE QIANLANRHL GIGFDQLLLV ETSNTKNVDF 

        70         80         90        100        110        120 
RYVIYNADGL EVEQCGNGAR CFAFFVSKKG LSNNNPIVVE TRSGIINLYL NDDNTVRVDM 

       130        140        150        160        170        180 
GKPSFNPADI LLLVPQQSTY YQIEGFDLGA VSIGNPHCVM LVEDVNTVDV SSIALRIQQS 

       190        200        210        220        230        240 
ELLPNQANIG FMQILNTHEI NLRVYERGSG ETLACGSGAC AAVVYGVEQG LLKENVVAHL 

       250        260        270 
NGGDTLIEYI QGGHVFLSGP VQFVFEGKVE I 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL02302.1.
RefSeqYP_903773.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AWJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02302; ABL02302; Rmag_0550.
GeneID4555074.
KEGGrma:Rmag_0550.
PATRIC32000789. VBICanRut45856_0613.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCRUT413404:GHM7-570-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPF_RUTMC
AccessionPrimary (citable) accession number: A1AWJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 51 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