MTHR_ORYSJ
ID MTHR_ORYSJ Reviewed; 594 AA.
AC Q75HE6; Q75GR7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable methylenetetrahydrofolate reductase;
DE EC=1.5.1.20;
GN OrderedLocusNames=Os03g0815200, LOC_Os03g60090;
GN ORFNames=OSJNBa0024F18.2, OSJNBb0042K11.1;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH;
CC Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.20;
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=1.5.1.20;
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 (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK121351; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC135594; AAR89836.1; -; Genomic_DNA.
DR EMBL; AC139172; AAR01748.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS87029.1; -; Genomic_DNA.
DR EMBL; AK062082; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK099527; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK121351; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015630556.1; XM_015775070.1.
DR AlphaFoldDB; Q75HE6; -.
DR SMR; Q75HE6; -.
DR STRING; 4530.OS03T0815200-01; -.
DR PaxDb; Q75HE6; -.
DR PRIDE; Q75HE6; -.
DR EnsemblPlants; Os03t0815200-01; Os03t0815200-01; Os03g0815200.
DR GeneID; 4334554; -.
DR Gramene; Os03t0815200-01; Os03t0815200-01; Os03g0815200.
DR KEGG; osa:4334554; -.
DR eggNOG; KOG0564; Eukaryota.
DR HOGENOM; CLU_025841_2_2_1; -.
DR InParanoid; Q75HE6; -.
DR OMA; HPVHGWG; -.
DR OrthoDB; 338303at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q75HE6; baseline and differential.
DR Genevisible; Q75HE6; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0106313; F:methylenetetrahydrofolate reductase NADPH 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 InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR004621; Fadh2_euk.
DR InterPro; IPR003171; Mehydrof_redctse-like.
DR Pfam; PF02219; MTHFR; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
DR TIGRFAMs; TIGR00677; fadh2_euk; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..594
FT /note="Probable methylenetetrahydrofolate reductase"
FT /id="PRO_0000190252"
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"
FT CONFLICT 5
FT /note="E -> G (in Ref. 4; AK121351)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="G -> R (in Ref. 4; AK099527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 66431 MW; C576C748AA847A18 CRC64;
MKVIEKIQEA AADGRTVFSF EYFPPKTEEG LDNLFERMDR MVAHGPNFCD ITWGAGGSTA
DLTLEIANRM QNMVCVETMM HLTCTNMPVE KIDDALTTIK SNGIQNVLAL RGDPPHGQDK
FVQVAGGFAC ALDLVQHIRA KYGDYFGITV AGYPEAHPDA IQSTEGATPE AYSNDLAYLK
QKVDAGADLI ITQLFYDTDI FLKFVNDCRQ IGITCPIVPG IMPINNYKGF LRMTGFCKTK
IPAEITAALE PIKDNEEAVK AYGIHLGTEM CKKILATGIK TLHLYTLNME KSALGILMNL
GLIEESKISR SLPWRPPTNV FRVKEDVRPI FWANRPKSYI SRTLGWDQYP HGRWGDSRNP
SYGALTDYQF TRPRGRGKKL QEEWAVPVKS VEDINERFMN FCQGKLTSSP WSELDGLQPE
TKIIDDQLVK INQKGFLTIN SQPAVNGERS DSTSVGWGGP GGYVYQKAYL EFFCSKEKLD
QLIEKSKAFP SLTYIAVNKD GESFSNIPTN AVNAVTWGVF PGKEIVQPTV VDSASFMVWK
DEAFEIWSKG WACLFPEGDS SREILDKVQK SYFLVSLVDN DYINGDLFAA FKEI
