ID METF_PECCC Reviewed; 298 AA. AC P71319; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-SEP-2023, entry version 87. DE RecName: Full=5,10-methylenetetrahydrofolate reductase; DE EC=1.5.1.54 {ECO:0000250|UniProtKB:P0AEZ1}; GN Name=metF; OS Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. OS carotovora). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=555; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=71; RA Calcutt M.J., Lewis M.S., Eisenstark A.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADH-dependent reduction of 5,10- CC methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to CC provide the methyl group necessary for methionine synthetase to convert CC homocysteine to methionine; the methyl group is given by 5- CC methyltetrahydrofolate. {ECO:0000250|UniProtKB:P0AEZ1}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10- CC methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH; CC Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.54; CC Evidence={ECO:0000250|UniProtKB:P0AEZ1}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19823; CC Evidence={ECO:0000250|UniProtKB:P0AEZ1}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P0AEZ1}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway. {ECO:0000250|UniProtKB:P0AEZ1}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U74302; AAC72242.1; -; Genomic_DNA. DR AlphaFoldDB; P71319; -. DR SMR; P71319; -. DR UniPathway; UPA00051; -. DR UniPathway; UPA00193; -. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR CDD; cd00537; MTHFR; 1. DR Gene3D; 3.20.20.220; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse-like. DR InterPro; IPR004620; MTHF_reductase_bac. DR NCBIfam; TIGR00676; fadh2; 1. DR PANTHER; PTHR45754; METHYLENETETRAHYDROFOLATE REDUCTASE; 1. DR PANTHER; PTHR45754:SF3; METHYLENETETRAHYDROFOLATE REDUCTASE; 1. DR Pfam; PF02219; MTHFR; 1. DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; FAD; Flavoprotein; Methionine biosynthesis; NAD; KW Oxidoreductase. FT CHAIN 1..298 FT /note="5,10-methylenetetrahydrofolate reductase" FT /id="PRO_0000190262" FT ACT_SITE 28 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 59 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 60 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 88 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 118 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 119 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 120 FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:18608" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 120 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 132 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 152 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 156 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 159 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 165 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 168 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 172 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 183 FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:18608" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 183 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 219 FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:18608" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" FT BINDING 279 FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:18608" FT /evidence="ECO:0000250|UniProtKB:P0AEZ1" SQ SEQUENCE 298 AA; 33589 MW; 50FE729E4E3E2C56 CRC64; MSFFHANQRE ALNQSLAELQ GRINVSFEFF PPRTSDMEET LWSSIDRLSS LKPKFVSVTY GANSGERDRT HSIIKTIKER TGLEAAPHLT CIDASREQLR EIAQDYWESG IRHIVALRGD LPQEGGKPDM YAADLVSLLK EVGDFDISVA AYPEVHPEAK SAQADLINLK HKIDAGANRA ITQFFFDVES YLRFRDRCVA TGIDVEIVPG ILPVSNFKQL QKFATMTNVR VPNWMTTMFD GLDNDPETRK MVGASIAMDM VKILSREGVK DFHFYTLNRA ELSYAICHTL GVRPDVAR //