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Q59487 (DYR_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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:
Dihydrofolate reductase

EC=1.5.1.3
Gene names
Name:folA
Synonyms:dhfR
Ordered Locus Names:LL1150
ORF Names:L162872
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) [Reference proteome] [HAMAP]
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.

Sequence similarities

Belongs to the dihydrofolate reductase family.

Contains 1 DHFR (dihydrofolate reductase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Dihydrofolate reductase
PRO_0000186394

Regions

Domain1 – 164164DHFR
Nucleotide binding6 – 72NADP By similarity
Nucleotide binding14 – 196NADP By similarity
Nucleotide binding43 – 464NADP By similarity
Nucleotide binding63 – 664NADP By similarity
Nucleotide binding99 – 1046NADP By similarity
Region5 – 73Substrate binding By similarity

Sites

Binding site271Substrate By similarity
Binding site581Substrate By similarity
Binding site1181Substrate By similarity

Experimental info

Sequence conflict111A → Q in CAA43094. Ref.1
Sequence conflict291Q → K in CAA43094. Ref.1
Sequence conflict721D → E in CAA43094. Ref.1
Sequence conflict901H → Y in CAA43094. Ref.1
Sequence conflict931N → D in CAA43094. Ref.1
Sequence conflict1251K → Q in CAA43094. Ref.1
Sequence conflict132 – 1332ST → TH in CAA43094. Ref.1
Sequence conflict1381R → K in CAA43094. Ref.1
Sequence conflict1411L → V in CAA43094. Ref.1
Sequence conflict1451K → I in CAA43094. Ref.1
Sequence conflict1541S → A in CAA43094. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59487 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 0BB4D97167F247F4

FASTA16819,729
        10         20         30         40         50         60 
MIIGIWAEDE AGLIGEADKM PWSLPAEQQH FKETTMNQVI LMGRKTFEGM NKRVLPGRIS 

        70         80         90        100        110        120 
IILTRDETYQ SDNEKVLIMH SPKEVLDWYH KQNKDLFITG GAEILALFES ELELLYRTVV 

       130        140        150        160 
HEKFKGDTYF PSTFDFGRFK LVSEKFHDKD ERNSYTFTIK KYEKVKQP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and molecular analysis of the dihydrofolate reductase gene from Lactococcus lactis."
Leszczynska K., Bolhuis A., Leenhouts K., Venema G., Ceglowski P.
Appl. Environ. Microbiol. 61:561-566(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 51-MG/7.
[2]"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IL1403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60681 Genomic DNA. Translation: CAA43094.1.
AE005176 Genomic DNA. Translation: AAK05248.1.
PIRF86768.
S47467.
RefSeqNP_267306.1. NC_002662.1.

3D structure databases

ProteinModelPortalQ59487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272623.L162872.

Chemistry

ChEMBLCHEMBL4012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK05248; AAK05248; L162872.
GeneID1114791.
KEGGlla:L162872.
PATRIC22294642. VBILacLac136773_1229.

Phylogenomic databases

eggNOGCOG0262.
HOGENOMHOG000040233.
KOK00287.
OMAIGIMAVD.
OrthoDBEOG6KT2V2.

Enzyme and pathway databases

BioCycLLAC272623:GHSH-1231-MONOMER.
UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFPIRSF000194. DHFR. 1 hit.
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDYR_LACLA
AccessionPrimary (citable) accession number: Q59487
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: May 14, 2014
This is version 98 of the entry and version 2 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