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B8FSD4 (DAPF_DESHD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:Dhaf_3907
OrganismDesulfitobacterium hafniense (strain DCB-2 / DSM 10664) [Complete proteome] [HAMAP]
Taxonomic identifier272564 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

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_1000124411

Regions

Region8 – 92Substrate binding By similarity
Region74 – 763Substrate binding By similarity
Region214 – 2152Substrate binding By similarity
Region224 – 2252Substrate binding By similarity

Sites

Active site741Proton donor/acceptor By similarity
Active site2231Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site471Substrate By similarity
Binding site651Substrate By similarity
Binding site1631Substrate By similarity
Binding site1961Substrate By similarity
Site1651Important for catalytic activity By similarity
Site2141Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond74 ↔ 223 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B8FSD4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 6D12D739AED191F3

FASTA28330,935
        10         20         30         40         50         60 
MEIVKMHGLG NDFVFIDHFQ GAPAELPDYP ELARKLCHRQ FGVGGDGLIM VLPSDKADAR 

        70         80         90        100        110        120 
MRILNSDGSE PEMCGNGIRC FARYIYDQGY VSQNPLQVET LAGILTLQLS ITGDQVTGVR 

       130        140        150        160        170        180 
VDMGEPILKS EQVPVLIQGD PVVGARLDVD GQEFEFTAVS MGNPHCVLFV EDYETLDFER 

       190        200        210        220        230        240 
IGPAIEKHPL FPRKTNVEFI IVNSPRELTM KVWERGAGPT LACGTGACAS VVAAVLNGRT 

       250        260        270        280 
ERKVTVHLPG GDLLIEWGED NRVYMTGPAA YVFKGVLLED ALS 

« Hide

References

[1]"Complete sequence of Desulfitobacterium hafniense DCB-2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Madsen T., Christiansen N., Ahring B., Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DCB-2 / DSM 10664.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001336 Genomic DNA. Translation: ACL21922.1.
RefSeqYP_002460358.1. NC_011830.1.

3D structure databases

ProteinModelPortalB8FSD4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272564.Dhaf_3907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL21922; ACL21922; Dhaf_3907.
GeneID7260928.
KEGGdhd:Dhaf_3907.
PATRIC21665821. VBIDesHaf15223_4067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAFMRIYNT.
OrthoDBEOG6ND0M5.
ProtClustDBCLSK2466407.

Enzyme and pathway databases

BioCycDHAF272564:GCV8-3984-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_DESHD
AccessionPrimary (citable) accession number: B8FSD4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 33 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