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Q7V7M5 (DAPF_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:PMT_0716
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length303 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 – 303303Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000077701

Regions

Region12 – 132Substrate binding By similarity
Region81 – 833Substrate binding By similarity
Region220 – 2212Substrate binding By similarity
Region230 – 2312Substrate binding By similarity

Sites

Active site811Proton donor/acceptor By similarity
Active site2291Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site531Substrate By similarity
Binding site721Substrate By similarity
Binding site1691Substrate By similarity
Binding site2021Substrate By similarity
Site1711Important for catalytic activity By similarity
Site2201Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond81 ↔ 229 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q7V7M5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 55D2D70E12958C9E

FASTA30332,747
        10         20         30         40         50         60 
MLVMLQFSKY QGLGNDFLLI DGREDQLTQQ VINPDPAWVR KICDRHFGIG ADGLILALPP 

        70         80         90        100        110        120 
RADGDLRMQI FNADGSLAEM CGNGIRCLTR FLADIEGDLC VQRWNIETLA GIICPVLQED 

       130        140        150        160        170        180 
GQICVDMGTP FLDPESIPTT LTIGSAGLPQ GECHLGSTSL HVAAVGMGNP HLIVPVEDLE 

       190        200        210        220        230        240 
NIPFENWGQR LEKHHAFPAK TNVHFLKIHS PNQLEIRVWE RGSGPTLACG TGACASLVAT 

       250        260        270        280        290        300 
CLLGLSDDHA EVLLPGGVLQ ISWPGRRGSV FMTGPAEPIF DGVLTPLLSP SHAEVLPQDD 


QII 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20891.1.
RefSeqNP_894548.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V7M5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT0716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20891; CAE20891; PMT_0716.
GeneID1728549.
KEGGpmt:PMT0716.
PATRIC23009409. VBIProMar135351_0859.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMALIVEPPY.
OrthoDBEOG6ND0M5.

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. 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_PROMM
AccessionPrimary (citable) accession number: Q7V7M5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 70 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