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Q9KVL6 (DAPF_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:VC_0126
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length276 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.

Sequence caution

The sequence AAF93303.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from sequence or structural similarity Ref.1. Source: TIGR

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from sequence or structural similarity Ref.1. Source: TIGR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149875

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region210 – 2112Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2191Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1591Substrate By similarity
Binding site1921Substrate By similarity
Site1611Important for catalytic activity By similarity
Site2101Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 219 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q9KVL6 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 8FCFEC10E5DD714B

FASTA27630,651
        10         20         30         40         50         60 
MHFHFSKMHG LGNDFMVVDC ITQNVFFSPE LIRRLADRHT GVGFDQLLVV EAPYDPESDF 

        70         80         90        100        110        120 
HYRIFNADGS EVEQCGNGAR CFARFVRMKG LTNKYTIHVS TKKGKMVLNV EEEDLITVNM 

       130        140        150        160        170        180 
GVPEFEPNKI PFRAKQSEKT YILRVGEHTL FCGAVSMGNP HVVTVVDDIR TAAVETLGPL 

       190        200        210        220        230        240 
LESHERFPER VNAGFMQVVS RDEINLRVYE RGAGETQACG SGACAAVAVG ILQGLLDEQV 

       250        260        270 
RVHLPGGELE IHWQGPGKPL YMTGPATHIY DGQISC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF93303.1. Different initiation.
PIRG82360.
RefSeqNP_229784.2. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KVL6.
SMRQ9KVL6. Positions 4-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0126.

Protocols and materials databases

DNASU2614550.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93303; AAF93303; VC_0126.
GeneID2614550.
KEGGvch:VC0126.
PATRIC20079296. VBIVibCho83274_0117.

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMACFARFVL.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

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_VIBCH
AccessionPrimary (citable) accession number: Q9KVL6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 6, 2002
Last modified: February 19, 2014
This is version 74 of the entry and version 2 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