ID   FOLD1_ROSDO             Reviewed;         300 AA.
AC   Q167Y9;
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 1;
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=folD1; OrderedLocusNames=RD1_2105;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000362; ABG31704.1; -; Genomic_DNA.
DR   RefSeq; YP_682390.1; -.
DR   GeneID; 4196651; -.
DR   GenomeReviews; CP000362_GR; RD1_2105.
DR   KEGG; rde:RD1_2105; -.
DR   NMPDR; fig|375451.6.peg.1965; -.
DR   HOGENOM; Q167Y9; -.
DR   OMA; Q167Y9; ISCTPAG.
DR   BioCyc; RDEN375451:RD1_2105-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; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
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    300       Bifunctional protein folD 1.
FT                                /FTId=PRO_0000268482.
SQ   SEQUENCE   300 AA;  31313 MW;  ED4ED50BBF8BFDD1 CRC64;
     MSATLIDGKA FAARVRAQVA EHVTRLKADH GITPGLAVVL VGQDPASQVY VRSKGKQTTE
     VGMKSVEHKL DADTSETDLL AVVDQLNKDP DIHGILVQLP LPGHLDEDLV INSIAPEKDV
     DGFHISNVGL LGTGQKSMVP CTPLGCLMML RDYHGSLLGM DAVVVGRSNI VGKPMAQLLL
     GDSCTVTIAH SRTKDLADVV RRADIVVAAV GRPEMVPGDW IKPGATVIDV GINRLDAPEK
     GEGKTRLVGD VDFDSCAAVA GAITPVPGGV GPMTIACLLA NTVTACCRAN GLEEPEGLTA
//