ID FOLD2_PSEPG Reviewed; 303 AA. AC B0KLM9; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 16-JUN-2009, entry version 9. 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=PputGB1_2105; OS Pseudomonas putida (strain GB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76869; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.; RT "Complete sequence of Pseudomonas putida GB-1."; RL Submitted (JAN-2008) 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; CP000926; ABY98006.1; -; Genomic_DNA. DR RefSeq; YP_001668342.1; -. DR GeneID; 5869894; -. DR GenomeReviews; CP000926_GR; PputGB1_2105. DR KEGG; ppg:PputGB1_2105; -. DR OMA; B0KLM9; MQIIDGK. 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 1 303 Bifunctional protein folD 2. FT /FTId=PRO_0000340591. SQ SEQUENCE 303 AA; 32148 MW; 250DDB49D2466032 CRC64; MNALTSLKLI DGKATAARVL AEVREQVQEL RQGGVQPGLV VVLVGADAAS QVYVRNKVLR AEEVGIRSQE HRLPADTTQA HLLTLIDRLN RDPEVNGILV QLPLPAHIDE HCVLQAINPL KDVDGFHSEN VGGLAQGRDV LTPCTPSGCM RLLRDACGEL RGKHAVVVGR SNIVGKPMAA LLLQADCTVT VVHSRSRDLP ALCRQADILV AAVGKPRLIG ADCLKPGAVV IDVGINRINE DGQNHLVGDV DFAAALPQVA GITPVPGGVG PMTIAYLMKN TLLALDLQQQ AAHQERTACL SPC //