ID FOLD2_DESHY Reviewed; 284 AA. AC Q24UZ7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. 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=DSY2356; OS Desulfitobacterium hafniense (strain Y51). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=138119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006; RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Inatomi K., Furukawa K., Inui M., Yukawa H.; RT "Complete genome sequence of the dehalorespiring bacterium RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides RT ethenogenes 195."; RL J. Bacteriol. 188:2262-2274(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. 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; AP008230; BAE84145.1; -; Genomic_DNA. DR RefSeq; YP_518589.1; -. DR GeneID; 3956871; -. DR GenomeReviews; AP008230_GR; DSY2356. DR KEGG; dsy:DSY2356; -. DR NMPDR; fig|138119.3.peg.2356; -. DR HOGENOM; Q24UZ7; -. DR OMA; Q24UZ7; VDAGINE. DR BioCyc; DHAF138119:DSY2356-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 1 284 Bifunctional protein folD 2. FT /FTId=PRO_0000268336. SQ SEQUENCE 284 AA; 30323 MW; 8774DFEE712CE028 CRC64; MAQLLDGKEI SKVLKEEIKE EVKRWKEQGV NPKLAVVLVG DDPASVVYAK SKQKVSDSLG IDFELTVLPA DSSEESILAL IDSLNANPDV HGIMIELPLP KHISKERVMA AVRPDKDVDG VHPINRGYIL SGEEGLFPAT PESCIEIMLR SGVEIAGKHV VIVGRGETVG KPLVFLILKH NATVTICHSR TPDLGAFTRQ ADIIVAAVGK AKLVKKDMVK PGAIVVDAGI NEIPGGICGD VDFEEVKEVA SLISPVPGGV GSLTTALIMK NVLKGITLQR KEGQ //