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F2JNN0 (F2JNN0_CELLD) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Diaminopimelate epimerase HAMAP-Rule MF_00197
Short name=DAP epimerase HAMAP-Rule MF_00197
EC=5.1.1.7 HAMAP-Rule MF_00197
Gene names
Name:dapF HAMAP-Rule MF_00197
Ordered Locus Names:Clole_4247
OrganismCellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5) (Clostridium lentocellum) [Complete proteome] [HAMAP] EMBL ADZ85919.1
Taxonomic identifier642492 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Lachnospiraceae › Cellulosilyticum ›

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 SAAS SAAS001653

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 SAAS SAAS001653

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197 SAAS SAAS001653.

Sequence similarities

Belongs to the diaminopimelate epimerase family. HAMAP-Rule MF_00197

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region10 – 112Substrate binding By similarity HAMAP-Rule MF_00197
Region73 – 753Substrate binding By similarity HAMAP-Rule MF_00197
Region213 – 2142Substrate binding By similarity HAMAP-Rule MF_00197
Region223 – 2242Substrate binding By similarity HAMAP-Rule MF_00197

Sites

Active site731Proton donor/acceptor By similarity HAMAP-Rule MF_00197
Active site2221Proton donor/acceptor By similarity HAMAP-Rule MF_00197
Binding site131Substrate By similarity HAMAP-Rule MF_00197
Binding site461Substrate By similarity HAMAP-Rule MF_00197
Binding site641Substrate By similarity HAMAP-Rule MF_00197
Binding site1621Substrate By similarity HAMAP-Rule MF_00197
Binding site1951Substrate By similarity HAMAP-Rule MF_00197
Site1641Important for catalytic activity By similarity HAMAP-Rule MF_00197
Site2131Important for catalytic activity By similarity HAMAP-Rule MF_00197

Amino acid modifications

Disulfide bond73 ↔ 222Size: 249-333 By similarity HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
F2JNN0 [UniParc].

Last modified May 31, 2011. Version 1.
Checksum: C309C7B2E82AED33

FASTA28331,377
        10         20         30         40         50         60 
MKINFTKMHG IGNDYVYVDG FKQTLKDPNA FSEFISDRHF GIGSDGLVII LPSEIADFRM 

        70         80         90        100        110        120 
RMFNADGSEG KMCGNATRCI GKFVYETGYT DKKNISLETL SGIKYLTLTV EDGKVVYVEV 

       130        140        150        160        170        180 
DMGKAILSPQ DIPVISDQET FINTPISIDN EIYYGTCVSM GNPHVVVYCE DVDLLSLESI 

       190        200        210        220        230        240 
GPKFEFNPLF PERINTEFVQ IIDDSTVKMR VWERGSGETW ACGTGACAVA VSCVLNGYCK 

       250        260        270        280 
INEEITVKLR GGDLKITYKE DGTVLMKGPA TKVFDGTIEY EEA

« Hide

References

[1]"Complete genome sequence of the cellulose-degrading bacterium Cellulosilyticum lentocellum."
US DOE Joint Genome Institute
Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C., Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S., Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G., Angert E.R., Currie C.R.
J. Bacteriol. 193:2357-2358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002582 Genomic DNA. Translation: ADZ85919.1.
RefSeqYP_004311117.1. NC_015275.1.

3D structure databases

ProteinModelPortalF2JNN0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ85919; ADZ85919; Clole_4247.
GeneID10334002.
KEGGcle:Clole_4247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01778.

Enzyme and pathway databases

BioCycCCLO642492:GIWK-4391-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF2JNN0_CELLD
AccessionPrimary (citable) accession number: F2JNN0
Entry history
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: April 3, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info