ID   DYR_BACSU               Reviewed;         168 AA.
AC   P11045;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Dihydrofolate reductase;
DE            EC=1.5.1.3;
GN   Name=dfrA; OrderedLocusNames=BSU21810;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8 AND
RP   166-168.
RC   STRAIN=ATCC 33712 / MI112;
RX   MEDLINE=88284366; PubMed=2840350; DOI=10.1016/0378-1119(88)90476-3;
RA   Iwakura M., Kawata M., Tsuda K., Tanaka T.;
RT   "Nucleotide sequence of the thymidylate synthase B and dihydrofolate
RT   reductase genes contained in one Bacillus subtilis operon.";
RL   Gene 64:9-20(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg;
RX   PubMed=8969496;
RA   Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT   "Organization of the Bacillus subtilis 168 chromosome between kdg and
RT   the attachment site of the SP beta prophage: use of long accurate PCR
RT   and yeast artificial chromosomes for sequencing.";
RL   Microbiology 142:3005-3015(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC       dihydrofolate + NADPH.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       tetrahydrofolate from dihydrofolate: step 1/1.
CC   -!- MISCELLANEOUS: The reaction catalyzed by this enzyme represents an
CC       essential step for de novo glycine and purine synthesis, DNA
CC       precursor synthesis, and for the conversion of dUMP to dTMP.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC   -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.
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DR   EMBL; M20012; AAA22853.1; -; Genomic_DNA.
DR   EMBL; L77246; AAA96635.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14099.1; -; Genomic_DNA.
DR   PIR; JT0291; RDBSD.
DR   RefSeq; NP_390064.1; -.
DR   HSSP; P00379; 1DHI.
DR   GeneID; 939091; -.
DR   GenomeReviews; AL009126_GR; BSU21810.
DR   KEGG; bsu:BSU21810; -.
DR   NMPDR; fig|224308.1.peg.2187; -.
DR   SubtiList; BG10795; dfrA.
DR   HOGENOM; P11045; -.
DR   OMA; P11045; LAHFKRT.
DR   BioCyc; BSUB224308:BSU2182-MON; -.
DR   BRENDA; 1.5.1.3; 150.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR001796; DHFR_reg.
DR   InterPro; IPR017925; Dihydrofolate_reductase_CS.
DR   PANTHER; PTHR11549:SF1; DHFR; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PRINTS; PR00070; DHFR.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; NADP;
KW   One-carbon metabolism; Oxidoreductase.
FT   CHAIN         1    168       Dihydrofolate reductase.
FT                                /FTId=PRO_0000186382.
FT   DOMAIN        1    159       DHFR.
FT   VARIANT     165    165       A -> V (in strain: MI112).
SQ   SEQUENCE   168 AA;  19176 MW;  6E4D11D03F630A44 CRC64;
     MISFIFAMDA NRLIGKDNDL PWHLPNDLAY FKKITSGHSI IMGRKTFESI GRPLPNRKNI
     VVTSAPDSEF QGCTVVSSLK DVLDICSGPE ECFVIGGAQL YTDLFPYADR LYMTKIHHEF
     EGDRHFPEFD ESNWKLVSSE QGTKDEKNPY DYEFLMYEKK NSSKAGGF
//