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Q1GPI7 (DAPF_SPHAL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Sala_2730
OrganismSphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) [Complete proteome] [HAMAP]
Taxonomic identifier317655 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingopyxis

Protein attributes

Sequence length268 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 – 268268Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011972

Regions

Region10 – 112Substrate binding By similarity
Region73 – 753Substrate binding By similarity
Region199 – 2002Substrate binding By similarity
Region209 – 2102Substrate binding By similarity

Sites

Active site731Proton donor/acceptor By similarity
Active site2081Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site641Substrate By similarity
Binding site1481Substrate By similarity
Binding site1811Substrate By similarity
Site1501Important for catalytic activity By similarity
Site1991Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond73 ↔ 208 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q1GPI7 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 6E8B6B31D8058712

FASTA26828,391
        10         20         30         40         50         60 
MADRFTKMHG LGNDFVVIDA RVAPVEMTPA RAHAIADRRH GIGCDQLILL EPSTSADVKM 

        70         80         90        100        110        120 
RIFNADGGEV EACGNATRCV ATLIGKPAVI ETLAGMLRVT PADGGAEVTL GEPVFDWDHI 

       130        140        150        160        170        180 
PLAMPMDTRD MPVAWDELEH GAAVNVGNPH IVFFVPEADA VALDQLGPRI ETDPLFPERV 

       190        200        210        220        230        240 
NVNVASLDGE NQLQLRVWER GVGLTQACGT GACATAVAAI RAGLVRSPVT VALPGGDLVI 

       250        260 
RWAPGEPIVM SGAATRVFDG ETDWAQFG 

« Hide

References

[1]"Complete sequence of chromosome of Sphingopyxis alaskensis RB2256."
US DOE Joint Genome Institute
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., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Chertkov O., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F., Ting L.M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13593 / LMG 18877 / RB2256.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000356 Genomic DNA. Translation: ABF54435.1.
RefSeqYP_617768.1. NC_008048.1.

3D structure databases

ProteinModelPortalQ1GPI7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING317655.Sala_2730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF54435; ABF54435; Sala_2730.
GeneID4082469.
KEGGsal:Sala_2730.
PATRIC23694820. VBISphAla23391_2819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSALA317655:GHHY-2770-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_SPHAL
AccessionPrimary (citable) accession number: Q1GPI7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 57 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