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P46151 (MTHR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylenetetrahydrofolate reductase 1

EC=1.5.1.20
Gene names
Name:MET12
Ordered Locus Names:YPL023C
ORF Names:LPB8C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion.

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MET13P531282EBI-11567,EBI-11572

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Methylenetetrahydrofolate reductase 1
PRO_0000190255

Regions

Nucleotide binding18 – 236NAD By similarity
Nucleotide binding49 – 502NAD and FAD By similarity
Nucleotide binding108 – 1103FAD By similarity
Nucleotide binding129 – 1302FAD By similarity

Sites

Active site181Proton donor/acceptor By similarity
Binding site781FAD By similarity
Binding site1101Substrate By similarity
Binding site1521FAD By similarity
Binding site1711FAD By similarity
Binding site1781FAD By similarity
Binding site1891Substrate By similarity
Binding site2861Substrate By similarity

Amino acid modifications

Modified residue1201Phosphoserine Ref.6
Modified residue3011Phosphoserine Ref.6
Modified residue3581Phosphoserine Ref.7

Experimental info

Sequence conflict110 – 1112DP → NL in K02070. Ref.3
Sequence conflict115 – 1162ED → VV in K02070. Ref.3
Sequence conflict1191D → V in K02070. Ref.3
Sequence conflict124 – 1318ESPFKYAV → RLLNMRLF in K02070. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P46151 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: D75612EA92D67500

FASTA65773,942
        10         20         30         40         50         60 
MSIRDLYHAR ASPFISLEFF PPKTELGTRN LMERMHRMTA LDPLFITVTW GAGGTTAEKT 

        70         80         90        100        110        120 
LTLASLAQQT LNIPVCMHLT CTNTEKAIID DALDRCYNAG IRNILALRGD PPIGEDWLDS 

       130        140        150        160        170        180 
QSNESPFKYA VDLVRYIKQS YGDKFCVGVA AYPEGHCEGE AEGHEQDPLK DLVYLKEKVE 

       190        200        210        220        230        240 
AGADFVITQL FYDVEKFLTF EMLFRERISQ DLPLFPGLMP INSYLLFHRA AKLSHASIPP 

       250        260        270        280        290        300 
AILSRFPPEI QSDDNAVKSI GVDILIELIQ EIYQRTSGRI KGFHFYTLNL EKAIAQIVSQ 

       310        320        330        340        350        360 
SPVLSHIVNE SSEEEGEDET SGEIGSIENV PIEDADGDIV LDDSNEETVA NRKRRRHSSL 

       370        380        390        400        410        420 
DSAKLIFNRA IVTEKGLRYN NENGSMPSKK ALISISKGHG TLGRDATWDE FPNGRFGDSR 

       430        440        450        460        470        480 
SPAYGEIDGY GPSIKVSKSK ALELWGIPKT IGDLKDIFIK YLEGSTDAIP WSDLGLSAET 

       490        500        510        520        530        540 
ALIQEELIQL NYRGYLTLAS QPATNATLSS DKIFGWGPAK GRLYQKAFVE MFIHRQQWET 

       550        560        570        580        590        600 
TLKPKLDHYG RRKFSYYAGD SSGSFETNLD PHSSSVVTWG VFPNSPVKQT TIIEEESFKA 

       610        620        630        640        650 
WRDEAFSIWS EWAKLFPRNT PANILLRLVH KDYCLVSIVH HDFKETDELW EMLLDQA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S., Matthews R.G., Rozen R.
Nat. Genet. 7:551-551(1994) [PubMed] [Europe PMC] [Abstract]
[6]"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].
[7]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36624 Genomic DNA. Translation: AAB68164.1.
K02070 Genomic DNA. No translation available.
BK006949 Genomic DNA. Translation: DAA11405.1.
PIRS63459.
RefSeqNP_015302.1. NM_001183837.1.

3D structure databases

ProteinModelPortalP46151.
SMRP46151. Positions 1-300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36154. 50 interactions.
DIPDIP-2825N.
IntActP46151. 5 interactions.
MINTMINT-1699985.
STRING4932.YPL023C.

Proteomic databases

MaxQBP46151.
PaxDbP46151.
PeptideAtlasP46151.
PRIDEP46151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL023C; YPL023C; YPL023C.
GeneID856084.
KEGGsce:YPL023C.

Organism-specific databases

CYGDYPL023c.
SGDS000005944. MET12.

Phylogenomic databases

eggNOGCOG0685.
HOGENOMHOG000246234.
KOK00297.
OMANVTWGAG.
OrthoDBEOG7M0P15.

Enzyme and pathway databases

BioCycYEAST:YPL023C-MONOMER.
UniPathwayUPA00193.

Gene expression databases

GenevestigatorP46151.

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...

Other

NextBio981098.

Entry information

Entry nameMTHR1_YEAST
AccessionPrimary (citable) accession number: P46151
Secondary accession number(s): D6W3Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways