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A0LUZ5 (DAPF_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Acel_1483
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length303 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 – 303303Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000077688

Regions

Region106 – 1083Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site1061Proton donor/acceptor By similarity
Active site2361Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site471Substrate By similarity
Binding site971Substrate By similarity
Binding site1781Substrate By similarity
Binding site2091Substrate By similarity
Site1801Important for catalytic activity By similarity
Site2271Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond106 ↔ 236 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
A0LUZ5 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 3DBBBFB454EFDFE0

FASTA30332,002
        10         20         30         40         50         60 
MDDVPFLKGH ATRNDFVILP DHDDELELDA ALVRAICDRR RGLGADGILR VVAVPADDAP 

        70         80         90        100        110        120 
VSSAGATADA AAGRPPQPSA GRPPQPAAAR WFMDYRNADG SVAEICGNGI RLFARYLVDA 

       130        140        150        160        170        180 
GLEEAGRFLV GTRIGPVPVD VPPAGDVTAW LPAPELRGGG RARFDGRMLE GVRVSVGNPH 

       190        200        210        220        230        240 
LVCVVDTLAD VDFTRAPVLD SDEFPDGANV EVVEIERPGV LRMRVYERGV GETWSCGSGA 

       250        260        270        280        290        300 
CAVAAVAEGA ERIPRPADGW WRIVVPGGEL RIRFDGDRVA LAGPAVVVAE GRLHLAALEK 


SDG 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK53255.1.
RefSeqYP_873241.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LUZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351607.Acel_1483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK53255; ABK53255; Acel_1483.
GeneID4485400.
KEGGace:Acel_1483.
PATRIC20673496. VBIAciCel132453_1576.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMAGNPHTVV.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycACEL351607:GIXW-1517-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_ACIC1
AccessionPrimary (citable) accession number: A0LUZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 50 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