ID FOLD2_SYNWW Reviewed; 272 AA. AC Q0AWX5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 18. 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=Swol_1474; OS Syntrophomonas wolfei subsp. wolfei (strain Goettingen). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=335541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Sims D., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., RA Sieber J., Stams A.J.M., Richardson P.; RT "Complete sequence of Syntrophomonas wolfei subsp. wolfei str. RT Goettingen."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000448; ABI68779.1; -; Genomic_DNA. DR RefSeq; YP_754150.1; -. DR GeneID; 4282339; -. DR GenomeReviews; CP000448_GR; Swol_1474. DR KEGG; swo:Swol_1474; -. DR HOGENOM; Q0AWX5; -. DR OMA; Q0AWX5; DVVYETA. 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 1 272 Bifunctional protein folD 2. FT /FTId=PRO_0000268540. SQ SEQUENCE 272 AA; 29705 MW; 934297BA64716B37 CRC64; MLIYGKDIRE QIKERVRQSA EEVKMGLAII RVGDDPSSMA YVRGIRKFAE ETGVKVEIVN LPDAVGEREL LKTIGDLNNS SEITGIMLQT PLPASLNASH LVNAIDFDKD VEGIHNYNLG KLISKEEGVR PCTPKAVISM LKAHDILIEG QKVTIIGRSM TVGSPLALMM TAENATVTVC HTRTRNLKEE ALRADILVAA VGKREFVTAD MVHKDMVVID VGINFDENGK MLGDVHEEAR NHCRLASAVP GGIGVITVAE LFDNLRILSQ KA //