ID FOLD1_PSEPG Reviewed; 290 AA. AC B0KJG3; 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 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=PputGB1_1899; 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; ABY97802.1; -; Genomic_DNA. DR RefSeq; YP_001668138.1; -. DR GeneID; 5869684; -. DR GenomeReviews; CP000926_GR; PputGB1_1899. DR KEGG; ppg:PputGB1_1899; -. DR OMA; B0KJG3; 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 1 290 Bifunctional protein folD 1. FT /FTId=PRO_0000340590. SQ SEQUENCE 290 AA; 31263 MW; D7D4EE5C9B393D5A CRC64; MVNHASMTAH LIDGKAIAAS LRQQIAQRVV ERRQQGLRTP GLAVILVGTD PASQVYVSHK RKDCEEVGFI SQAFDLPSET TQQALTELID RLNDDPAVDG ILLQLPLPAH LDASLLLERI RPDKDVDGFH PYNIGRLAQR IPLLRPCTPK GIMTLLESTG QDLYGMNAVI VGASNIVGRP MAMELLLAGC TVTVCHRFTK DLAGHVGRAD LVVVAAGKPG LVKGEWVKEG AIVIDVGINR QEDGKLVGDV VYETALPRAG WITPVPGGVG PMTRACLLEN TLYAAEELHK //