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Q21P78 (DAPF_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:Sde_0237
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

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_1000011957

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region211 – 2122Substrate binding By similarity
Region221 – 2222Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2201Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1601Substrate By similarity
Binding site1931Substrate By similarity
Site1621Important for catalytic activity By similarity
Site2111Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 220 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q21P78 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 8D4FB99814117036

FASTA27729,528
        10         20         30         40         50         60 
MRLRFTKMHG LGNDFVMIDA ISQRVTITPE RARQLADRHF GVGCDQVLVV ETPDSPDADF 

        70         80         90        100        110        120 
KYRIFNHDGS EVENCGNGAR CFAVFVRQRG LTAKSVITVE TAVGRMVLHV QEDDQVTVDM 

       130        140        150        160        170        180 
GAPILSPADI PLAAPQQATS YTLPTQGAGD ITIGAVSMGN PHAVYCVNDC KTAPVETLGP 

       190        200        210        220        230        240 
EIEAHPHFPK KVNAGFMQVV SPSEINLRVY ERGAGETLAC GTGACAAVVA GRLQGLLENT 

       250        260        270 
VKVNLPGGSL SITWEGVDSP VMMTGPATTV FHGQVKI 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD79501.1.
RefSeqYP_525713.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21P78.
SMRQ21P78. Positions 3-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_0237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD79501; ABD79501; Sde_0237.
GeneID3968079.
KEGGsde:Sde_0237.
PATRIC23399103. VBISacDeg56404_0259.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSDEG203122:GI2M-238-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_SACD2
AccessionPrimary (citable) accession number: Q21P78
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 55 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