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Protein

Methylenetetrahydrofolate reductase 1

Gene

MET12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FADBy similarity

Pathway:itetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei18 – 181Proton donor/acceptorBy similarity
Binding sitei78 – 781FADBy similarity
Binding sitei110 – 1101SubstrateBy similarity
Binding sitei152 – 1521FADBy similarity
Binding sitei171 – 1711FADBy similarity
Binding sitei178 – 1781FADBy similarity
Binding sitei189 – 1891SubstrateBy similarity
Binding sitei286 – 2861SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 236NADBy similarity
Nucleotide bindingi49 – 502NAD and FADBy similarity
Nucleotide bindingi108 – 1103FADBy similarity
Nucleotide bindingi129 – 1302FADBy similarity

GO - Molecular functioni

  • methylenetetrahydrofolate reductase (NAD(P)H) activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciYEAST:YPL023C-MONOMER.
ReactomeiREACT_324954. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylenetetrahydrofolate reductase 1 (EC:1.5.1.20)
Gene namesi
Name:MET12
Ordered Locus Names:YPL023C
ORF Names:LPB8C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

CYGDiYPL023c.
EuPathDBiFungiDB:YPL023C.
SGDiS000005944. MET12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657Methylenetetrahydrofolate reductase 1PRO_0000190255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei301 – 3011Phosphoserine1 Publication
Modified residuei358 – 3581Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46151.
PaxDbiP46151.
PeptideAtlasiP46151.
PRIDEiP46151.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MET13P531282EBI-11567,EBI-11572

Protein-protein interaction databases

BioGridi36154. 51 interactions.
DIPiDIP-2825N.
IntActiP46151. 5 interactions.
MINTiMINT-1699985.

Structurei

3D structure databases

ProteinModelPortaliP46151.
SMRiP46151. Positions 1-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000246234.
InParanoidiP46151.
KOiK00297.
OMAiNVTWGAG.
OrthoDBiEOG7M0P15.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
TIGRFAMsiTIGR00677. fadh2_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

P46151-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIRDLYHAR ASPFISLEFF PPKTELGTRN LMERMHRMTA LDPLFITVTW
60 70 80 90 100
GAGGTTAEKT LTLASLAQQT LNIPVCMHLT CTNTEKAIID DALDRCYNAG
110 120 130 140 150
IRNILALRGD PPIGEDWLDS QSNESPFKYA VDLVRYIKQS YGDKFCVGVA
160 170 180 190 200
AYPEGHCEGE AEGHEQDPLK DLVYLKEKVE AGADFVITQL FYDVEKFLTF
210 220 230 240 250
EMLFRERISQ DLPLFPGLMP INSYLLFHRA AKLSHASIPP AILSRFPPEI
260 270 280 290 300
QSDDNAVKSI GVDILIELIQ EIYQRTSGRI KGFHFYTLNL EKAIAQIVSQ
310 320 330 340 350
SPVLSHIVNE SSEEEGEDET SGEIGSIENV PIEDADGDIV LDDSNEETVA
360 370 380 390 400
NRKRRRHSSL DSAKLIFNRA IVTEKGLRYN NENGSMPSKK ALISISKGHG
410 420 430 440 450
TLGRDATWDE FPNGRFGDSR SPAYGEIDGY GPSIKVSKSK ALELWGIPKT
460 470 480 490 500
IGDLKDIFIK YLEGSTDAIP WSDLGLSAET ALIQEELIQL NYRGYLTLAS
510 520 530 540 550
QPATNATLSS DKIFGWGPAK GRLYQKAFVE MFIHRQQWET TLKPKLDHYG
560 570 580 590 600
RRKFSYYAGD SSGSFETNLD PHSSSVVTWG VFPNSPVKQT TIIEEESFKA
610 620 630 640 650
WRDEAFSIWS EWAKLFPRNT PANILLRLVH KDYCLVSIVH HDFKETDELW

EMLLDQA
Length:657
Mass (Da):73,942
Last modified:October 1, 1996 - v2
Checksum:iD75612EA92D67500
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1112DP → NL in K02070 (PubMed:6095044).Curated
Sequence conflicti115 – 1162ED → VV in K02070 (PubMed:6095044).Curated
Sequence conflicti119 – 1191D → V in K02070 (PubMed:6095044).Curated
Sequence conflicti124 – 1318ESPFKYAV → RLLNMRLF in K02070 (PubMed:6095044).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36624 Genomic DNA. Translation: AAB68164.1.
K02070 Genomic DNA. No translation available.
BK006949 Genomic DNA. Translation: DAA11405.1.
PIRiS63459.
RefSeqiNP_015302.1. NM_001183837.1.

Genome annotation databases

EnsemblFungiiYPL023C; YPL023C; YPL023C.
GeneIDi856084.
KEGGisce:YPL023C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36624 Genomic DNA. Translation: AAB68164.1.
K02070 Genomic DNA. No translation available.
BK006949 Genomic DNA. Translation: DAA11405.1.
PIRiS63459.
RefSeqiNP_015302.1. NM_001183837.1.

3D structure databases

ProteinModelPortaliP46151.
SMRiP46151. Positions 1-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36154. 51 interactions.
DIPiDIP-2825N.
IntActiP46151. 5 interactions.
MINTiMINT-1699985.

Proteomic databases

MaxQBiP46151.
PaxDbiP46151.
PeptideAtlasiP46151.
PRIDEiP46151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL023C; YPL023C; YPL023C.
GeneIDi856084.
KEGGisce:YPL023C.

Organism-specific databases

CYGDiYPL023c.
EuPathDBiFungiDB:YPL023C.
SGDiS000005944. MET12.

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000246234.
InParanoidiP46151.
KOiK00297.
OMAiNVTWGAG.
OrthoDBiEOG7M0P15.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciYEAST:YPL023C-MONOMER.
ReactomeiREACT_324954. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi981098.
PROiP46151.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
TIGRFAMsiTIGR00677. fadh2_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Molecular cloning and nucleotide sequence analysis of the Saccharomyces cerevisiae RAD1 gene."
    Yang E., Friedberg E.C.
    Mol. Cell. Biol. 4:2161-2169(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
  4. "Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification."
    Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S., Matthews R.G., Rozen R.
    Nat. Genet. 7:195-200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMTHR1_YEAST
AccessioniPrimary (citable) accession number: P46151
Secondary accession number(s): D6W3Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.