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O80585 (MTHR2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylenetetrahydrofolate reductase 2

Short name=AtMTHFR2
EC=1.5.1.20
Gene names
Name:MTHFR2
Ordered Locus Names:At2g44160
ORF Names:F6E13.29
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length594 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.2

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.2

Pathway

One-carbon metabolism; tetrahydrofolate interconversion.

Subunit structure

Homodimer By similarity. Ref.2

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Methylenetetrahydrofolate reductase 2
PRO_0000190250

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

Experimental info

Sequence conflict721N → S in CAB53783. Ref.1
Sequence conflict1151P → H in AAK43892. Ref.5
Sequence conflict5081A → V in CAB53783. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O80585 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: E2F4F919FCE10EF8

FASTA59466,802
        10         20         30         40         50         60 
MKVIDKIQSL ADEGKTAFSF EFFPPKTEDG VDNLFERMDR MVAYGPTFCD ITWGAGGSTA 

        70         80         90        100        110        120 
DLTLDIASRM QNVVCVESMM HLTCTNMPVE KIDHALETIR SNGIQNVLAL RGDPPHGQDK 

       130        140        150        160        170        180 
FVQVEGGFDC ALDLVNHIRS KYGDYFGITV AGYPEAHPDV IGENGLASNE AYQSDLEYLK 

       190        200        210        220        230        240 
KKIDAGADLI VTQLFYDTDI FLKFVNDCRQ IGISCPIVPG IMPINNYRGF LRMTGFCKTK 

       250        260        270        280        290        300 
IPVEVMAALE PIKDNEEAVK AYGIHLGTEM CKKMLAHGVK SLHLYTLNME KSALAILMNL 

       310        320        330        340        350        360 
GMIDESKISR SLPWRRPANV FRTKEDVRPI FWANRPKSYI SRTKGWEDFP QGRWGDSRSA 

       370        380        390        400        410        420 
SYGALSDHQF SRPRARDKKL QQEWVVPLKS VEDIQEKFKE LCLGNLKSSP WSELDGLQPE 

       430        440        450        460        470        480 
TRIINEQLIK VNSKGFLTIN SQPSVNAERS DSPTVGWGGP VGYVYQKAYL EFFCSKEKLD 

       490        500        510        520        530        540 
AVVEKCKALP SITYMAVNKG EQWVSNTAQA DVNAVTWGVF PAKEIIQPTI VDPASFNVWK 

       550        560        570        580        590 
DEAFETWSRS WANLYPEADP SRNLLEEVKN SYYLVSLVEN DYINGDIFAV FADL 

« Hide

References

« Hide 'large scale' references
[1]"Folate metabolism in higher plants: cloning of a cDNA for 5,10-methylenetetrahydrofolate reductase in Arabidopsis thaliana."
Ravanel S., Rebeille F., Douce R.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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], FUNCTION, SUBUNIT, ENZYME REGULATION.
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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].
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-594.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245414 mRNA. Translation: CAB53783.1.
AF181967 mRNA. Translation: AAD55788.1.
AC004005 Genomic DNA. Translation: AAC23420.2.
CP002685 Genomic DNA. Translation: AEC10384.1.
AY050434 mRNA. Translation: AAK91450.1.
AF370515 mRNA. Translation: AAK43892.1.
AK220952 mRNA. Translation: BAD94483.1.
PIRT00696.
RefSeqNP_566011.1. NM_129979.2.
UniGeneAt.11693.
At.23509.

3D structure databases

ProteinModelPortalO80585.
SMRO80585. Positions 18-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4358. 1 interaction.
IntActO80585. 1 interaction.

Proteomic databases

PaxDbO80585.
PRIDEO80585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G44160.1; AT2G44160.1; AT2G44160.
GeneID819022.
KEGGath:AT2G44160.

Organism-specific databases

GeneFarm5158. 490.
TAIRAT2G44160.

Phylogenomic databases

eggNOGCOG0685.
HOGENOMHOG000246234.
InParanoidO80585.
KOK00297.
OMANDDLTYH.
PhylomeDBO80585.

Enzyme and pathway databases

BioCycARA:AT2G44160-MONOMER.
UniPathwayUPA00193.

Gene expression databases

GenevestigatorO80585.

Family and domain databases

Gene3D3.20.20.220. 1 hit.
InterProIPR029041. FAD-linked_oxidoreductase-like.
IPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamPF02219. MTHFR. 1 hit.
[Graphical view]
SUPFAMSSF51730. SSF51730. 1 hit.
TIGRFAMsTIGR00677. fadh2_euk. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTHR2_ARATH
AccessionPrimary (citable) accession number: O80585
Secondary accession number(s): Q56ZL2 expand/collapse secondary AC list , Q94JZ1, Q9SE59, Q9SUJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 2, 2002
Last modified: June 11, 2014
This is version 108 of the entry and version 2 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