Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B4U9P0 (DAPF_HYDS0) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 41. 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:HY04AAS1_1165
OrganismHydrogenobaculum sp. (strain Y04AAS1) [Complete proteome] [HAMAP]
Taxonomic identifier380749 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeHydrogenobaculum

Protein attributes

Sequence length277 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 – 277277Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099243

Regions

Region81 – 833Substrate binding By similarity
Region207 – 2082Substrate binding By similarity
Region218 – 2192Substrate binding By similarity

Sites

Active site811Proton donor/acceptor By similarity
Active site2171Proton donor/acceptor By similarity
Binding site111Substrate By similarity
Binding site521Substrate By similarity
Binding site721Substrate By similarity
Binding site1891Substrate By similarity
Site1551Important for catalytic activity By similarity
Site2071Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond81 ↔ 217 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B4U9P0 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 2A43015B831A96A9

FASTA27730,932
        10         20         30         40         50         60 
MLITKYQGSG NDFIIIDNRD NFVYKEIEKL GLSINEFVRK LCEQHTSVGA DGVILIEKAR 

        70         80         90        100        110        120 
NTKNHFSWAF FNADGSAAEM CGNGSRCAAR FAYEKDIAPK DIVFETIAGE IEAHIMDSKR 

       130        140        150        160        170        180 
VKVQLTPYHS HQKNIEIKTE YGTFKGHFVN TGVPHFVIFV DEDELDNLDV EKVGRAIRYH 

       190        200        210        220        230        240 
EYFAPKGTNV NFVAKTKNGS FRIRTYERGV EGETLACGTG SAACGINAYL LGLSASNIVD 

       250        260        270 
IITKSGELLK ITIENDKVFL EGPTTKVFEG MLSYEIF 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y04AAS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001130 Genomic DNA. Translation: ACG57851.1.
RefSeqYP_002121829.1. NC_011126.1.

3D structure databases

ProteinModelPortalB4U9P0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380749.HY04AAS1_1165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG57851; ACG57851; HY04AAS1_1165.
GeneID6743982.
KEGGhya:HY04AAS1_1165.
PATRIC22137028. VBIHydSp64203_1172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycHSP380749:GH30-1204-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_HYDS0
AccessionPrimary (citable) accession number: B4U9P0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: June 11, 2014
This is version 41 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