ID FOLD1_RHILO Reviewed; 299 AA. AC Q989A7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 16-JUN-2009, entry version 37. 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=mlr6508; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). 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; BA000012; BAB52790.1; -; Genomic_DNA. DR RefSeq; NP_107004.1; -. DR HSSP; P11586; 1A4I. DR GeneID; 1229659; -. DR GenomeReviews; BA000012_GR; mlr6508. DR KEGG; mlo:mlr6508; -. DR NMPDR; fig|266835.1.peg.5105; -. DR HOGENOM; Q989A7; -. DR OMA; Q989A7; HSKTRDL. DR BRENDA; 1.5.1.5; 3315. DR BRENDA; 3.5.4.9; 3315. 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; 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 1 299 Bifunctional protein folD 1. FT /FTId=PRO_0000268463. SQ SEQUENCE 299 AA; 30891 MW; 2674A552499480F3 CRC64; MAEVIDGKSV AEDVVRTVKA LTAELVAKGK AKPGLAVVIV GEDPASQVYV ASKSRTAKEC GFHSLQHTLP AETSEEALLK IIADLNADPA VNGILVQLPL PAHIDAGKII QAIAPQKDVD GFHFINVGKL GTGELDTAFV PCTPAGSMLL IQRVRGKDLS GLNAVVVGRS NIVGKPMANL LLAANCTVTI AHSRTKDLPA LARTADILVA AVGRPEMIKG DWVKPGATVI DVGINRIPAP EKGEGKSRLV GDVAYAEAAR QAGAITPVPG GVGPMTIAML MANTLASAYL AAGLKRPTF //