Q9SE94 (MTHR1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Methylenetetrahydrofolate reductase 1 EC=1.5.1.20 Alternative name(s): ZmMTHFR1
Organism	Zea mays (Maize)
Taxonomic identifier	4577 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › Liliopsida › Petrosaviidae › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	593 AA.
Sequence status	Complete.
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 interconversion.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	methionine metabolic process Inferred from electronic annotation. Source: InterPro tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	methylenetetrahydrofolate reductase (NAD(P)H) activity Inferred from electronic annotation. Source: UniProtKB-EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 593	593	Methylenetetrahydrofolate reductase 1		PRO_0000190251
Regions
	Nucleotide binding	21 – 26	6	NAD By similarity
	Nucleotide binding	52 – 53	2	NAD and FAD By similarity
	Nucleotide binding	111 – 113	3	FAD By similarity
	Nucleotide binding	157 – 160	4	FAD By similarity
Sites
	Active site	21	1	Proton donor/acceptor By similarity
	Binding site	81	1	FAD By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	153	1	FAD By similarity
	Binding site	175	1	FAD By similarity
	Binding site	182	1	FAD By similarity
	Binding site	193	1	Substrate By similarity
	Binding site	285	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SE94 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4568996775B638B4	FASTA	593	66,429
	10 20 30 40 50 60 MKVIEKILEA AGDGRTAFSF EYFPPKTEEG VENLFERMDR MVAHGPSFCD ITWGAGGSTA 70 80 90 100 110 120 DLTLEIANRM QNMVCVETMM HLTCTNMPVE KIDHALETIK SNGIQNVLAL RGDPPHGQDK 130 140 150 160 170 180 FVQVEGGFAC ALDLVQHIRA KYGDYFGITV AGYPEAHPDA IQGEGGATLE AYSNDLAYLK 190 200 210 220 230 240 RKVDAGADLI VTQLFYDTDI FLKFVNDCRQ IGITCPIVPG IMPINNYKGF LRMTGFCKTK 250 260 270 280 290 300 IPSEITAALD PIKDNEEAVR QYGIHLGTEM CKKILATGIK TLHLYTLNMD KSAIGILMNL 310 320 330 340 350 360 GLIEESKVSR PLPWRPATNV FRVKEDVRPI FWANRPKSYL KRTLGWDQYP HGRWGDSRNP 370 380 390 400 410 420 SYGALTDHQF TRPRGRGKKL QEEWAVPLKS VEDISERFTN FCQGKLTSSP WSELDGLQPE 430 440 450 460 470 480 TKIIDDQLVN INQKGFLTIN SQPAVNGEKS DSPTVGWGGP GGYVYQKAYL EFFCAKEKLD 490 500 510 520 530 540 QLIEKIKAFP SLTYIAVNKD GETFSNISPN AVNAVTWGVF PGKEIIQPTV VDHASFMVWK 550 560 570 580 590 DEAFEIWTRG WGCMFPEGDS SRELLEKVQK TYYLVSLVDN DYVQGDLFAA FKI

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], FUNCTION, ENZYME REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF174486 mRNA. Translation: AAD51733.1.
RefSeq	NP_001104947.1. NM_001111477.1.
UniGene	Zm.475.
3D structure databases
ProteinModelPortal	Q9SE94.
ModBase	Search...
MobiDB	Search...
Proteomic databases
PRIDE	Q9SE94.
ProMEX	Q9SE94.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	541794.
KEGG	zma:541794.
Organism-specific databases
Gramene	Q9SE94.
MaizeGDB	146840.
Phylogenomic databases
HOGENOM	HOG000246234.
KO	K00297.
OMA	YLEFFVS.
Enzyme and pathway databases
UniPathway	UPA00193.
Family and domain databases
Gene3D	3.20.20.220. 1 hit.
InterPro	IPR029041. FAD-linked_oxidoreductase-like. IPR004621. Fadh2_euk. IPR003171. Mehydrof_redctse. [Graphical view]
Pfam	PF02219. MTHFR. 1 hit. [Graphical view]
SUPFAM	SSF51730. SSF51730. 1 hit.
TIGRFAMs	TIGR00677. fadh2_euk. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTHR1_MAIZE

Accession

Primary (citable) accession number: Q9SE94

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	May 1, 2000
Last modified:	July 9, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program