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Q97FV2 (DAPF_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:CA_C2624
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length333 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
Reference 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 – 333333Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149834

Regions

Region88 – 903Substrate binding By similarity
Region228 – 2292Substrate binding By similarity
Region238 – 2392Substrate binding By similarity

Sites

Active site881Proton donor/acceptor By similarity
Active site2371Proton donor/acceptor By similarity
Binding site241Substrate By similarity
Binding site611Substrate By similarity
Binding site791Substrate By similarity
Binding site1761Substrate By similarity
Binding site2101Substrate By similarity
Site1781Important for catalytic activity By similarity
Site2281Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond88 ↔ 237 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q97FV2 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 37CF1548F4B54A05

FASTA33337,528
        10         20         30         40         50         60 
MEINIREDAF IVEINILKCH GTGNDFILID EYNNNYNLDD ETRRDIAIQA CNRAKFIGGD 

        70         80         90        100        110        120 
GILFVQKSDI CDAKMRIFNA DGSEAEMCGN GLRCVGRYVI EMLNKESVEI ETLKSKYWVK 

       130        140        150        160        170        180 
LQEDIYEGVK TVKIDIKSVS LDVKTLPLNY KKEKLIFDKI PELSDEFDFT AVSITNPHLI 

       190        200        210        220        230        240 
AIVNNIDSDK LVEIGKKGNS TKSVLPQGVN VSFVKVIDSS NIYVKTYERG VGLTKSCGTA 

       250        260        270        280        290        300 
MTASSIVSCI GEKVQFDNAI NVYNDGGAIK TIVHKDSNGN YSVDFIGNAT FIFEGTMELD 

       310        320        330 
KRKIEQFTID ESKFEKETNS YNEFFEYTRK NCK 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK80571.1.
PIRH97222.
RefSeqNP_349231.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97FV2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C2624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK80571; AAK80571; CA_C2624.
GeneID1118807.
KEGGcac:CA_C2624.
PATRIC32039613. VBICloAce74127_2813.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCACE272562:GJIH-2679-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_CLOAB
AccessionPrimary (citable) accession number: Q97FV2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2001
Last modified: February 19, 2014
This is version 73 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