ID   FOLD3_ROSDO             Reviewed;         290 AA.
AC   Q160C0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Bifunctional protein folD 3;
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=folD3; OrderedLocusNames=RD1_4237;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter
OS   sp. (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17098896; DOI=10.1128/JB.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J.,
RA   Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C.,
RA   Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E.,
RA   Beatty J.T., Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG33673.1; -; Genomic_DNA.
DR   RefSeq; YP_684359.1; -.
DR   GeneID; 4195555; -.
DR   GenomeReviews; CP000362_GR; RD1_4237.
DR   KEGG; rde:RD1_4237; -.
DR   NMPDR; fig|375451.6.peg.3935; -.
DR   HOGENOM; Q160C0; -.
DR   OMA; Q160C0; SIGNIVY.
DR   BioCyc; RDEN375451:RD1_4237-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    290       Bifunctional protein folD 3.
FT                                /FTId=PRO_0000268484.
SQ   SEQUENCE   290 AA;  31020 MW;  2D5E16E1F76DD717 CRC64;
     MQDPRLLMGK PVRERILEEV RSVTEKVDRI GKLVSISIGD VPEVAVYVRN QARAASTAGL
     PFDQEFWGAD VTQDECKAMI QKMNDDPEVL GIILQRPVPD HINVRSLQSA IHPLKDVEGM
     NPASIGNIVY NDVAMAPCTA AAAVELIRET GLKLEGLEVV MVGHSEIVGK PAAMMLMAEG
     ATVTVCHHLT RSVAMHSRRA DVIVVAVGKA HLIGADMVKP GAAVIDIGIN QITEADGNTR
     IVGDVDTDAV KEIAGWVTPV PGGVGPVTVA ILMRNAVRAH ERQKAAGWYA
//