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Q5NNL4 (DAPF_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:ZMO1072
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length269 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 – 269269Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000011991

Regions

Region10 – 112Substrate binding By similarity
Region74 – 763Substrate binding By similarity
Region200 – 2012Substrate binding By similarity
Region210 – 2112Substrate binding By similarity

Sites

Active site741Proton donor/acceptor By similarity
Active site2091Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site651Substrate By similarity
Binding site1491Substrate By similarity
Binding site1821Substrate By similarity
Site1511Important for catalytic activity By similarity
Site2001Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond74 ↔ 209 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q5NNL4 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 5D4E577266EC2DE3

FASTA26929,297
        10         20         30         40         50         60 
MTFSFHKMHG LGNDFIVLDA RKNPIQMNPA LAQALSNRHT GIGCDQLIII GNGKNQADVS 

        70         80         90        100        110        120 
MEIWNADGSE VEACGNATRC VPVFLGRDVI ISTAAGLLDA RLSDEGACVD MGRPRLSWDE 

       130        140        150        160        170        180 
IPLAYAMDTL SMPVAWEDLK EPTAVNMGNP HVVFVVDDVD AVDFGRLGNM IEHDQLFPER 

       190        200        210        220        230        240 
INVNIVMVTG KDHLKMRTWE RGAGLTRACG TGACATFVAA KRRRLVSGKT QIDLPGGRLV 

       250        260 
LDENSEGHII MRGPATYVFK GEADWASFS 

« Hide

References

[1]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008692 Genomic DNA. Translation: AAV89696.1.
RefSeqYP_162807.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ5NNL4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89696; AAV89696; ZMO1072.
GeneID3188029.
KEGGzmo:ZMO1072.
PATRIC32567442. VBIZymMob102260_1016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
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_ZYMMO
AccessionPrimary (citable) accession number: Q5NNL4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 61 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