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Q9SE60 (MTHR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylenetetrahydrofolate reductase 1

Short name=AtMTHFR1
EC=1.5.1.20
Gene names
Name:MTHFR1
Ordered Locus Names:At3g59970
ORF Names:F24G16.240
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The probable reversibility of the MTHFR reaction in plants suggests that they can metabolize the methyl group of 5,10-methylenetetrahydrofolate to serine, sugars and starch. Ref.1

Catalytic activity

5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.

Cofactor

FAD By similarity.

Enzyme regulation

Plant MTHFRs strongly prefer NADH over NADPH. Not inhibited by methionine or S-adenosylmethionine. Ref.1

Pathway

One-carbon metabolism; tetrahydrofolate interconversion.

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmethionine biosynthetic process

Inferred from electronic annotation. Source: InterPro

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

   Molecular_functionmethylenetetrahydrofolate reductase (NAD(P)H) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9SE60-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9SE60-2)

The sequence of this isoform differs from the canonical sequence as follows:
     397-421: KFKELCIGNLKSSPWSELDGLQPET → VGFTLRTLVQIVSISFPHTHLHIFM
     422-592: Missing.
Note: Derived from EST data. May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Methylenetetrahydrofolate reductase 1
PRO_0000190249

Regions

Nucleotide binding21 – 266NAD By similarity
Nucleotide binding52 – 532NAD and FAD By similarity
Nucleotide binding111 – 1133FAD By similarity
Nucleotide binding157 – 1604FAD By similarity

Sites

Active site211Proton donor/acceptor By similarity
Binding site811FAD By similarity
Binding site1131Substrate By similarity
Binding site1531FAD By similarity
Binding site1751FAD By similarity
Binding site1821FAD By similarity
Binding site1931Substrate By similarity
Binding site2851Substrate By similarity

Natural variations

Alternative sequence397 – 42125KFKEL…LQPET → VGFTLRTLVQIVSISFPHTH LHIFM in isoform 2.
VSP_018093
Alternative sequence422 – 592171Missing in isoform 2.
VSP_018094

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 72D7453AF1AF1573

FASTA59266,288
        10         20         30         40         50         60 
MKVVDKIKSV TEQGQTAFSF EFFPPKTEDG VENLFERMDR LVSYGPTFCD ITWGAGGSTA 

        70         80         90        100        110        120 
DLTLEIASRM QNVICVETMM HLTCTNMPIE KIDHALETIR SNGIQNVLAL RGDPPHGQDK 

       130        140        150        160        170        180 
FVQVEGGFAC ALDLVNHIRS KYGDYFGITV AGYPEAHPDV IEADGLATPE SYQSDLAYLK 

       190        200        210        220        230        240 
KKVDAGADLI VTQLFYDTDI FLKFVNDCRQ IGINCPIVPG IMPISNYKGF LRMAGFCKTK 

       250        260        270        280        290        300 
IPAELTAALE PIKDNDEAVK AYGIHFATEM CKKILAHGIT SLHLYTLNVD KSAIGILMNL 

       310        320        330        340        350        360 
GLIDESKISR SLPWRRPANV FRTKEDVRPI FWANRPKSYI SRTKGWNDFP HGRWGDSHSA 

       370        380        390        400        410        420 
AYSTLSDYQF ARPKGRDKKL QQEWVVPLKS IEDVQEKFKE LCIGNLKSSP WSELDGLQPE 

       430        440        450        460        470        480 
TKIINEQLGK INSNGFLTIN SQPSVNAAKS DSPAIGWGGP GGYVYQKAYL EFFCSKDKLD 

       490        500        510        520        530        540 
TLVEKSKAFP SITYMAVNKS ENWVSNTGES DVNAVTWGVF PAKEVIQPTI VDPASFKVWK 

       550        560        570        580        590 
DEAFEIWSRS WANLYPEDDP SRKLLEEVKN SYYLVSLVDN NYINGDIFSV FA 

« Hide

Isoform 2 [UniParc].

Checksum: D53A9DAEE1233C18
Show »

FASTA42147,258

References

« Hide 'large scale' references
[1]"Isolation, characterization, and functional expression of cDNAs encoding NADH-dependent methylenetetrahydrofolate reductase from higher plants."
Roje S., Wang H., McNeil S.D., Raymond R.K., Appling D.R., Shachar-Hill Y., Bohnert H.J., Hanson A.D.
J. Biol. Chem. 274:36089-36096(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, ENZYME REGULATION.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF181966 mRNA. Translation: AAD55787.1.
AL138647 Genomic DNA. Translation: CAB75816.1.
CP002686 Genomic DNA. Translation: AEE79992.1.
CP002686 Genomic DNA. Translation: AEE79994.1.
AY122922 mRNA. Translation: AAM67455.1.
AY070034 mRNA. Translation: AAL49791.1.
PIRT47821.
RefSeqNP_191556.1. NM_115860.3.
NP_850723.1. NM_180392.1.
UniGeneAt.1168.
At.23509.
At.69007.
At.72842.

3D structure databases

ProteinModelPortalQ9SE60.
SMRQ9SE60. Positions 1-302.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9SE60.
PRIDEQ9SE60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G59970.3; AT3G59970.3; AT3G59970. [Q9SE60-1]
GeneID825167.
KEGGath:AT3G59970.

Organism-specific databases

GeneFarm5157. 490.
TAIRAT3G59970.

Phylogenomic databases

eggNOGCOG0685.
HOGENOMHOG000246234.
InParanoidQ9SE60.
KOK00297.
OMAYLEFFVS.
PhylomeDBQ9SE60.
ProtClustDBPLN02540.

Enzyme and pathway databases

BioCycARA:AT3G59970-MONOMER.
ARA:GQT-1418-MONOMER.
ARA:GQT-258-MONOMER.
UniPathwayUPA00193.

Gene expression databases

GenevestigatorQ9SE60.

Family and domain databases

InterProIPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
IPR004620. MTHF_reductase_bac.
[Graphical view]
PfamPF02219. MTHFR. 1 hit.
[Graphical view]
TIGRFAMsTIGR00676. fadh2. 1 hit.
TIGR00677. fadh2_euk. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTHR1_ARATH
AccessionPrimary (citable) accession number: Q9SE60
Secondary accession number(s): Q3EAG9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names