ID MTHR1_MAIZE Reviewed; 593 AA.
AC Q9SE94;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Methylenetetrahydrofolate reductase (NADH) 1;
DE EC=1.5.1.54 {ECO:0000269|PubMed:10593891};
DE AltName: Full=ZmMTHFR1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=10593891; DOI=10.1074/jbc.274.51.36089;
RA Roje S., Wang H., McNeil S.D., Raymond R.K., Appling D.R., Shachar-Hill Y.,
RA Bohnert H.J., Hanson A.D.;
RT "Isolation, characterization, and functional expression of cDNAs encoding
RT NADH-dependent methylenetetrahydrofolate reductase from higher plants.";
RL J. Biol. Chem. 274:36089-36096(1999).
CC -!- FUNCTION: The probable reversibility of the MTHFR reaction in plants
CC suggests that they can metabolize the methyl group of 5,10-
CC methylenetetrahydrofolate to serine, sugars and starch.
CC {ECO:0000269|PubMed:10593891}.
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:0000269|PubMed:10593891};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Plant MTHFRs strongly prefer NADH over NADPH. Not
CC inhibited by methionine or S-adenosylmethionine.
CC {ECO:0000269|PubMed:10593891}.
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; AF174486; AAD51733.1; -; mRNA.
DR RefSeq; NP_001104947.1; NM_001111477.2.
DR AlphaFoldDB; Q9SE94; -.
DR SMR; Q9SE94; -.
DR STRING; 4577.Q9SE94; -.
DR PaxDb; 4577-GRMZM2G347056_P01; -.
DR ProMEX; Q9SE94; -.
DR EnsemblPlants; Zm00001eb062180_T001; Zm00001eb062180_P001; Zm00001eb062180.
DR EnsemblPlants; Zm00001eb062180_T002; Zm00001eb062180_P002; Zm00001eb062180.
DR EnsemblPlants; Zm00001eb062180_T003; Zm00001eb062180_P003; Zm00001eb062180.
DR GeneID; 541794; -.
DR Gramene; Zm00001eb062180_T001; Zm00001eb062180_P001; Zm00001eb062180.
DR Gramene; Zm00001eb062180_T002; Zm00001eb062180_P002; Zm00001eb062180.
DR Gramene; Zm00001eb062180_T003; Zm00001eb062180_P003; Zm00001eb062180.
DR KEGG; zma:541794; -.
DR MaizeGDB; 146840; -.
DR eggNOG; KOG0564; Eukaryota.
DR HOGENOM; CLU_025841_2_2_1; -.
DR InParanoid; Q9SE94; -.
DR OMA; IGWDEFP; -.
DR OrthoDB; 1381745at2759; -.
DR BRENDA; 1.5.1.20; 6752.
DR BRENDA; 1.5.1.54; 6752.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q9SE94; baseline and differential.
DR Genevisible; Q9SE94; ZM.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IBA:GO_Central.
DR GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR CDD; cd00537; MTHFR; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR004621; Fadh2_euk.
DR InterPro; IPR003171; Mehydrof_redctse-like.
DR NCBIfam; TIGR00677; fadh2_euk; 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 1: Evidence at protein level;
KW FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..593
FT /note="Methylenetetrahydrofolate reductase (NADH) 1"
FT /id="PRO_0000190251"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 21..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 52..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 52..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 111..113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 593 AA; 66429 MW; 4568996775B638B4 CRC64;
MKVIEKILEA AGDGRTAFSF EYFPPKTEEG VENLFERMDR MVAHGPSFCD ITWGAGGSTA
DLTLEIANRM QNMVCVETMM HLTCTNMPVE KIDHALETIK SNGIQNVLAL RGDPPHGQDK
FVQVEGGFAC ALDLVQHIRA KYGDYFGITV AGYPEAHPDA IQGEGGATLE AYSNDLAYLK
RKVDAGADLI VTQLFYDTDI FLKFVNDCRQ IGITCPIVPG IMPINNYKGF LRMTGFCKTK
IPSEITAALD PIKDNEEAVR QYGIHLGTEM CKKILATGIK TLHLYTLNMD KSAIGILMNL
GLIEESKVSR PLPWRPATNV FRVKEDVRPI FWANRPKSYL KRTLGWDQYP HGRWGDSRNP
SYGALTDHQF TRPRGRGKKL QEEWAVPLKS VEDISERFTN FCQGKLTSSP WSELDGLQPE
TKIIDDQLVN INQKGFLTIN SQPAVNGEKS DSPTVGWGGP GGYVYQKAYL EFFCAKEKLD
QLIEKIKAFP SLTYIAVNKD GETFSNISPN AVNAVTWGVF PGKEIIQPTV VDHASFMVWK
DEAFEIWTRG WGCMFPEGDS SRELLEKVQK TYYLVSLVDN DYVQGDLFAA FKI
//
