Reviewed, UniProtKB/Swiss-Prot Q9SE60 (MTHR1_ARATH)

Names and origin

Protein names

Recommended name:
    Methylenetetrahydrofolate reductase 1
      Short name=AtMTHFR1
    EC=1.5.1.20

Gene names

Name:	MTHFR1
Ordered Locus Names:	At3g59970
ORF Names:	F24G16.240

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 pathway.
Subunit structure	Homodimer. Ref.1
Sequence similarities	Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methionine metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	methylenetetrahydrofolate reductase (NADPH) activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 592	592	Methylenetetrahydrofolate reductase 1		PRO_0000190249
Natural variations
	Alternative sequence	397 – 421	25	KFKEL…LQPET → VGFTLRTLVQIVSISFPHTH LHIFM in isoform 2.		VSP_018093
	Alternative sequence	422 – 592	171	Missing in isoform 2.		VSP_018094

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 72D7453AF1AF1573	FASTA	592	66,288
	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
	Isoform 2. Checksum: D53A9DAEE1233C18	FASTA	421	47,258
	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 IEDVQEVGFT LRTLVQIVSI SFPHTHLHIF M

References

	« Hide 'large scale' referencesShow '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: 10593891] [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. , 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: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF181966 mRNA. Translation: AAD55787.1. AL138647 Genomic DNA. Translation: CAB75816.1. AY122922 mRNA. Translation: AAM67455.1. AY070034 mRNA. Translation: AAL49791.1.
IPI	IPI00534913. IPI00544875.
PIR	T47821.
RefSeq	NP_191556.1. NP_850723.1.
UniGene	At.1168 At.23509 At.69007
3D structure databases
HSSP	HSSP built from PDB template 1B5T based on UniProtKB P00394.
ModBase	Search...
Proteomic databases
PRIDE	Q9SE60.
ProMEX	Q9SE60.
Genome annotation databases
GeneID	825167.
GenomeReviews	Gene locus AT3G59970 in contig BA000014_GR.
KEGG	ath:AT3G59970.
NMPDR	fig|3702.1.peg.17355.
Organism-specific databases
GeneFarm	5157. 490.
TAIR	At3g59970.
Phylogenomic databases
OMA	Q9SE60. DITWHPA.
Enzyme and pathway databases
BRENDA	1.5.1.20. 302.
Gene expression databases
ArrayExpress	Q9SE60.
Family and domain databases
InterPro	IPR004621. Fadh2_euk. IPR003171. Mehydrof_redctse. [Graphical view]
Pfam	PF02219. MTHFR. 1 hit. [Graphical view]
TIGRFAMs	TIGR00677. fadh2_euk. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTHR1_ARATH

Accession

Primary (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:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)