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B8GVW2 (DAPF_CAUCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:CCNA_03800
OrganismCaulobacter crescentus (strain NA1000 / CB15N) [Complete proteome] [HAMAP]
Taxonomic identifier565050 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length288 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 – 288288Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000124406

Regions

Region10 – 112Substrate binding By similarity
Region80 – 823Substrate binding By similarity
Region218 – 2192Substrate binding By similarity
Region228 – 2292Substrate binding By similarity

Sites

Active site801Proton donor/acceptor By similarity
Active site2271Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site511Substrate By similarity
Binding site711Substrate By similarity
Binding site1661Substrate By similarity
Binding site2001Substrate By similarity
Site1681Important for catalytic activity By similarity
Site2181Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond80 ↔ 227 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B8GVW2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 8E47AB6C103BAD88

FASTA28830,546
        10         20         30         40         50         60 
MSRTFLKMNG LGNDFVVIQT LTEAFDPTPE QIRAIAKRPG VDGKGGIGCD QVIAIDPPRA 

        70         80         90        100        110        120 
EGASAYVRFW NSDGEVAGAC GNGTRCVAWL LMQSAGKDAV AFDTVAGRLS GVAAGDKLVT 

       130        140        150        160        170        180 
VDMGPPGLDW TQIPLAEEMN TERVELQVGP IDAPLVHTPV CVSMGNPHVV FFVDAPVTDD 

       190        200        210        220        230        240 
FARGTGSLVE HHPLFPEGVN VGFAHIASRD HIRLKVWERG AGLTQACGTG ACAAQVAAVR 

       250        260        270        280 
RGLTDRKARV EFDTGSLTIE WRESDGHVIM TGPITMEYAG KLPELVAA 

« Hide

References

[1]"The genetic basis of laboratory adaptation in Caulobacter crescentus."
Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1000 / CB15N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001340 Genomic DNA. Translation: ACL97265.1.
RefSeqYP_002519173.1. NC_011916.1.

3D structure databases

ProteinModelPortalB8GVW2.
SMRB8GVW2. Positions 5-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190650.CC_3686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL97265; ACL97265; CCNA_03800.
GeneID7331998.
KEGGccs:CCNA_03800.
PATRIC21312087. VBICauCre52860_3704.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCAULONA1000:CCNA_03800-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_CAUCN
AccessionPrimary (citable) accession number: B8GVW2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 38 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