ID   FOLD2_RHOSR             Reviewed;         286 AA.
AC   Q0S375;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Bifunctional protein folD 2;
DE   Includes:
DE     RecName: Full=Methylenetetrahydrofolate dehydrogenase;
DE              EC=1.5.1.5;
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
DE              EC=3.5.4.9;
GN   Name=folD2; OrderedLocusNames=RHA1_ro06234;
OS   Rhodococcus sp. (strain RHA1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Catalyzes the oxidation of 5,10-
CC       methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and
CC       then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-
CC       formyltetrahydrofolate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) =
CC       5,10-methenyltetrahydrofolate + NADPH.
CC   -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
CC       formyltetrahydrofolate.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family.
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DR   EMBL; CP000431; ABG98011.1; -; Genomic_DNA.
DR   RefSeq; YP_706169.1; -.
DR   SMR; Q0S375; 3-280.
DR   GeneID; 4223785; -.
DR   GenomeReviews; CP000431_GR; RHA1_ro06234.
DR   KEGG; rha:RHA1_ro06234; -.
DR   HOGENOM; Q0S375; -.
DR   OMA; Q0S375; DVVYETA.
DR   BioCyc; RSP101510:RHA1_RO06234-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase act...; IEA:HAMAP.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NA...; IEA:HAMAP.
DR   GO; GO:0009396; P:folic acid and derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01576; -; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   ProDom; PD002300; THFDhg/Cyc_hydro; 1.
DR   PROSITE; PS00766; THF_DHG_CYH_1; FALSE_NEG.
DR   PROSITE; PS00767; THF_DHG_CYH_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW   Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
FT   CHAIN         1    286       Bifunctional protein folD 2.
FT                                /FTId=PRO_0000268471.
SQ   SEQUENCE   286 AA;  30097 MW;  BD9181AD66BCBA4F CRC64;
     MTATILDGKA TRDEIFEDLK VRVSALKDRG ITPGLGTVLV GDDPGSAAYV RGKHNDCAKV
     GITSIRRDLP GDITQEKLDA TIDELNANPD CTGYIVQLPL PKQLDENAAL ERIDPDKDAD
     GLHPVNLGRL VLGKKAPLPC TPRGILHLLR RYEVPIEGAH VVVVGRGVTV GRPIGLLFTR
     RSENATVTLC HTRTRDLGAE VRRADIVIAA AGVPGLITAD MVKPGAAVLD VGVSRTADGL
     RGDVAADVAE VAGFLSPNPG GVGPLTRAFL LTNVVERAER VAASLG
//