ID   DYR_MYCTU               Reviewed;         159 AA.
AC   P0A546; O33305;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=Dihydrofolate reductase;
DE            EC=1.5.1.3;
GN   Name=folA; Synonyms=dfrA; OrderedLocusNames=Rv2763c, MT2833;
GN   ORFNames=MTV002.28c;
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   MEDLINE=22206494; PubMed=12218036;
RX   DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   MEDLINE=20090935; PubMed=10623528; DOI=10.1006/jmbi.1999.3328;
RA   Li R., Sirawaraporn R., Chitnumsub P., Sirawaraporn W., Wooden J.,
RA   Athappilly F., Turley S., Hol W.G.J.;
RT   "Three-dimensional structure of M. tuberculosis dihydrofolate
RT   reductase reveals opportunities for the design of novel tuberculosis
RT   drugs.";
RL   J. Mol. Biol. 295:307-323(2000).
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; BX842580; CAA15559.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK47152.1; -; Genomic_DNA.
DR   PIR; B70881; B70881.
DR   RefSeq; NP_217279.1; -.
DR   RefSeq; NP_337338.1; -.
DR   PDB; 1DF7; X-ray; 1.70 A; A=1-159.
DR   PDB; 1DG5; X-ray; 2.00 A; A=1-159.
DR   PDB; 1DG7; X-ray; 1.80 A; A=1-159.
DR   PDB; 1DG8; X-ray; 2.00 A; A=1-159.
DR   PDB; 2CIG; X-ray; 1.90 A; A=1-159.
DR   PDBsum; 1DF7; -.
DR   PDBsum; 1DG5; -.
DR   PDBsum; 1DG7; -.
DR   PDBsum; 1DG8; -.
DR   PDBsum; 2CIG; -.
DR   GeneID; 887777; -.
DR   GeneID; 925455; -.
DR   GenomeReviews; AE000516_GR; MT2833.
DR   GenomeReviews; AL123456_GR; Rv2763c.
DR   KEGG; mtc:MT2833; -.
DR   KEGG; mtu:Rv2763c; -.
DR   TIGR; MT2833; -.
DR   TubercuList; Rv2763c; -.
DR   HOGENOM; P0A546; -.
DR   OMA; P0A546; WVIGGER.
DR   BRENDA; 1.5.1.3; 809.
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   3D-structure; Complete proteome; NADP; One-carbon metabolism;
KW   Oxidoreductase.
FT   CHAIN         1    159       Dihydrofolate reductase.
FT                                /FTId=PRO_0000186400.
FT   DOMAIN        1    158       DHFR.
FT   STRAND        2      9
FT   STRAND       12     16
FT   HELIX        25     35
FT   STRAND       38     43
FT   HELIX        44     49
FT   HELIX        52     54
FT   STRAND       60     65
FT   STRAND       76     81
FT   HELIX        82     85
FT   STRAND       88     93
FT   HELIX        97    103
FT   HELIX       104    106
FT   STRAND      108    115
FT   STRAND      136    139
FT   STRAND      150    157
SQ   SEQUENCE   159 AA;  17640 MW;  F17C038F1B773797 CRC64;
     MVGLIWAQAT SGVIGRGGDI PWRLPEDQAH FREITMGHTI VMGRRTWDSL PAKVRPLPGR
     RNVVLSRQAD FMASGAEVVG SLEEALTSPE TWVIGGGQVY ALALPYATRC EVTEVDIGLP
     REAGDALAPV LDETWRGETG EWRFSRSGLR YRLYSYHRS
//