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P11045 (DYR_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:dfrA
Ordered Locus Names:BSU21810
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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_0000186382

Regions

Domain1 – 159159DHFR
Nucleotide binding6 – 72NADP By similarity
Nucleotide binding14 – 196NADP By similarity
Nucleotide binding43 – 464NADP By similarity
Nucleotide binding62 – 654NADP By similarity
Nucleotide binding95 – 1006NADP By similarity
Region5 – 73Substrate binding By similarity

Sites

Binding site271Substrate By similarity
Binding site571Substrate By similarity
Binding site1141Substrate By similarity

Natural variations

Natural variant1651A → V in strain: MI112.

Sequences

Sequence LengthMass (Da)Tools
P11045 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 6E4D11D03F630A44

FASTA16819,176
        10         20         30         40         50         60 
MISFIFAMDA NRLIGKDNDL PWHLPNDLAY FKKITSGHSI IMGRKTFESI GRPLPNRKNI 

        70         80         90        100        110        120 
VVTSAPDSEF QGCTVVSSLK DVLDICSGPE ECFVIGGAQL YTDLFPYADR LYMTKIHHEF 

       130        140        150        160 
EGDRHFPEFD ESNWKLVSSE QGTKDEKNPY DYEFLMYEKK NSSKAGGF 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the thymidylate synthase B and dihydrofolate reductase genes contained in one Bacillus subtilis operon."
Iwakura M., Kawata M., Tsuda K., Tanaka T.
Gene 64:9-20(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8 AND 166-168.
Strain: ATCC 33712 / MI112.
[2]"Organization of the Bacillus subtilis 168 chromosome between kdg and the attachment site of the SP beta prophage: use of long accurate PCR and yeast artificial chromosomes for sequencing."
Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.
Microbiology 142:3005-3015(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20012 Genomic DNA. Translation: AAA22853.1.
L77246 Genomic DNA. Translation: AAA96635.1.
AL009126 Genomic DNA. Translation: CAB14099.1.
PIRRDBSD. JT0291.
RefSeqNP_390064.1. NC_000964.3.

3D structure databases

ProteinModelPortalP11045.
SMRP11045. Positions 1-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU21810.

Proteomic databases

PaxDbP11045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14099; CAB14099; BSU21810.
GeneID939091.
KEGGbsu:BSU21810.
PATRIC18976167. VBIBacSub10457_2274.

Organism-specific databases

GenoListBSU21810. [Micado]

Phylogenomic databases

eggNOGCOG0262.
HOGENOMHOG000040233.
KOK00287.
OMAFKALTMG.
OrthoDBEOG6KT2V2.
PhylomeDBP11045.

Enzyme and pathway databases

BioCycBSUB:BSU21810-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_BACSU
AccessionPrimary (citable) accession number: P11045
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 111 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList