ID FOLD1_SYNWW Reviewed; 277 AA. AC Q0AZF5; 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 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=Swol_0566; 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; ABI67899.1; -; Genomic_DNA. DR RefSeq; YP_753270.1; -. DR GeneID; 4281407; -. DR GenomeReviews; CP000448_GR; Swol_0566. DR KEGG; swo:Swol_0566; -. DR HOGENOM; Q0AZF5; -. DR OMA; Q0AZF5; PLATIMI. 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; 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 1 277 Bifunctional protein folD 1. FT /FTId=PRO_0000268539. SQ SEQUENCE 277 AA; 29604 MW; DADC92739574C92B CRC64; MEIISGSQIA QEIRQKLKEK NEREGISPCL AMILVGGQKE DLHYVGLKEK AATATGGKSR LLHLPEDTSQ QELMAKIAEL NQDEQVDGIL LQLPLPAALE EQTDEILAAI RPDKDVDGFS LVNRGRMSGD RPGFISCAAL ACLEVIERFF PSLAGKKAVL VGDSFDLIIP LATIMIKRAC QLSVLPSYEP GLASGADILV VEKGRAGIVQ AEGLAPGVLI IDAGFYWGAG GVCGNVDRAA LERQGFEARL LPVPGGMGPI LIAKLMENLA QAARQKR //