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Q9SE94 (MTHR1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1

EC=1.5.1.20
Alternative name(s):
ZmMTHFR1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length593 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 By similarity.

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Methylenetetrahydrofolate reductase 1
PRO_0000190251

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

Sequences

Sequence LengthMass (Da)Tools
Q9SE94 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4568996775B638B4

FASTA59366,429
        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 

« Hide

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.
RefSeqNP_001104947.1. NM_001111477.1.
UniGeneZm.475.

3D structure databases

ProteinModelPortalQ9SE94.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9SE94.
ProMEXQ9SE94.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID541794.
KEGGzma:541794.

Organism-specific databases

GrameneQ9SE94.
MaizeGDB146840.

Phylogenomic databases

HOGENOMHOG000246234.
KOK00297.
OMAYLEFFVS.

Enzyme and pathway databases

UniPathwayUPA00193.

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 nameMTHR1_MAIZE
AccessionPrimary (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 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