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Q0AIP0 (DAPF_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:Neut_0505
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length278 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 – 278278Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011915

Regions

Region10 – 112Substrate binding By similarity
Region77 – 793Substrate binding By similarity
Region212 – 2132Substrate binding By similarity
Region222 – 2232Substrate binding By similarity

Sites

Active site771Proton donor/acceptor By similarity
Active site2211Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site491Substrate By similarity
Binding site681Substrate By similarity
Binding site1611Substrate By similarity
Binding site1941Substrate By similarity
Site1631Important for catalytic activity By similarity
Site2121Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond77 ↔ 221 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q0AIP0 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 39078C56CE6D780A

FASTA27830,467
        10         20         30         40         50         60 
MKLQFTKMHG LGNDFIVINA INQPASLTFL DPATIRRLAD RHFGIGFDQL LIVEQAREGG 

        70         80         90        100        110        120 
DFRYRIFNAD GGEVEQCGNG ARCFARFVRD YNLTDKNTIR VETARGIITP TIENNGEVSV 

       130        140        150        160        170        180 
NMGVPQFEPA EIPFQAAQRM PVYPLQIGDK TIEISAVSIG NPHAVQIIPD IDLAPVTTEG 

       190        200        210        220        230        240 
PKIEAHPLFP ERVNAGFMQI IDRAHIRLRV FERGTGETLA CGTGACAAVV CGILRGLLDT 

       250        260        270 
TVQVAMHGGN LQIRWDGKDK PVWMTGPAIT VFEGTIDL 

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000450 Genomic DNA. Translation: ABI58781.1.
RefSeqYP_746746.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AIP0.
SMRQ0AIP0. Positions 3-278.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335283.Neut_0505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI58781; ABI58781; Neut_0505.
GeneID4272006.
KEGGnet:Neut_0505.
PATRIC22718027. VBINitEut7577_0687.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycNEUT335283:GHT6-517-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689. PTHR31689. 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_NITEC
AccessionPrimary (citable) accession number: Q0AIP0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: June 11, 2014
This is version 58 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