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P53128 (MTHR2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 116. 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 2

EC=1.5.1.20
Alternative name(s):
YmL45
Gene names
Name:MET13
Synonyms:MET11, MRPL45
Ordered Locus Names:YGL125W
ORF Names:G2882
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length600 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.

Miscellaneous

Present with 8600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Caution

Was originally (Ref.4) thought to be a mitochondrial ribosomal protein.

Sequence caution

The sequence CAA63833.1 differs from that shown. Reason: Sequencing errors.

The sequence CAA96833.1 differs from that shown. Reason: Sequencing errors.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MET12P461512EBI-11572,EBI-11567

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 600600Methylenetetrahydrofolate reductase 2
PRO_0000190256

Regions

Nucleotide binding22 – 276NAD By similarity
Nucleotide binding54 – 552NAD and FAD By similarity
Nucleotide binding114 – 1163FAD By similarity
Nucleotide binding133 – 1342FAD By similarity

Sites

Active site221Proton donor/acceptor By similarity
Binding site841FAD By similarity
Binding site1161Substrate By similarity
Binding site1561FAD By similarity
Binding site1711FAD By similarity
Binding site1781FAD By similarity
Binding site1891Substrate By similarity
Binding site2821Substrate By similarity

Experimental info

Sequence conflict41 – 422RM → LA AA sequence Ref.4
Sequence conflict481P → A AA sequence Ref.4
Sequence conflict731A → R in CAA63833. Ref.1
Sequence conflict152 – 1543GVA → RC in AAC99805. Ref.5
Sequence conflict1831Missing in AAC99805. Ref.5
Sequence conflict2111V → L in AAC99805. Ref.5
Sequence conflict233 – 24311GQISIPQHFSS → ANLHPSTFLV in AAC99805. Ref.5
Sequence conflict266 – 27611MCQKLLDSGYV → CVKIARQWLR in AAC99805. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P53128 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 470B0EFE4E2D1D75

FASTA60068,560
        10         20         30         40         50         60 
MKITEKLEQH RQTSGKPTYS FEYFVPKTTQ GVQNLYDRMD RMYEASLPQF IDITWNAGGG 

        70         80         90        100        110        120 
RLSHLSTDLV ATAQSVLGLE TCMHLTCTNM PISMIDDALE NAYHSGCQNI LALRGDPPRD 

       130        140        150        160        170        180 
AENWTPVEGG FQYAKDLIKY IKSKYGDHFA IGVAGYPECH PELPNKDVKL DLEYLKQKID 

       190        200        210        220        230        240 
AGGDFIITQM FYDVDNFINW CSQVRAAGMD VPIIPGIMPI TTYAAFLRRA QWGQISIPQH 

       250        260        270        280        290        300 
FSSRLDPIKD DDELVRDIGT NLIVEMCQKL LDSGYVSHLH IYTMNLEKAP LMILERLNIL 

       310        320        330        340        350        360 
PTESEFNAHP LAVLPWRKSL NPKRKNEEVR PIFWKRRPYS YVARTSQWAV DEFPNGRFGD 

       370        380        390        400        410        420 
SSSPAFGDLD LCGSDLIRQS ANKCLELWST PTSINDVAFL VINYLNGNLK CLPWSDIPIN 

       430        440        450        460        470        480 
DEINPIKAHL IELNQHSIIT INSQPQVNGI RSNDKIHGWG PKDGYVYQKQ YLEFMLPKTK 

       490        500        510        520        530        540 
LPKLIDTLKN NEFLTYFAID SQGDLLSNHP DNSKSNAVTW GIFPGREILQ PTIVEKISFL 

       550        560        570        580        590        600 
AWKEEFYHIL NEWKLNMNKY DKPHSAQFIQ SLIDDYCLVN IVDNDYISPD DQIHSILLSL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a putative methylenetetrahydrofolate reductase by sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII."
Tizon B., Rodriguez-Torres A.M., Rodriguez-Belmonte E., Cadahia J.L., Cerdan E.
Yeast 12:1047-1051(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification and characterization of the genes for mitochondrial ribosomal proteins of Saccharomyces cerevisiae."
Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S., Herfurth E., Wittmann-Liebold B., Nishimura T., Isono K.
Eur. J. Biochem. 245:449-456(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-49.
[5]Housen I., Lafontaine D., Belot N., Vandenhaute J.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-286.
Strain: ATCC 28383 / FL100 / VTT C-80102.
[6]"Saccharomyces cerevisiae expresses two genes encoding isozymes of methylenetetrahydrofolate reductase."
Raymond R.K., Kastanos E.K., Appling D.R.
Arch. Biochem. Biophys. 372:300-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo."
Roje S., Chan S.Y., Kaplan F., Raymond R.K., Horne D.W., Appling D.R., Hanson A.D.
J. Biol. Chem. 277:4056-4061(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]Erratum
Roje S., Chan S.Y., Kaplan F., Raymond R.K., Horne D.W., Appling D.R., Hanson A.D.
J. Biol. Chem. 277:36904-36904(2002)
Cited for: SEQUENCE REVISION TO 176-181; 197-198 AND 230.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z72647 Genomic DNA. Translation: CAA96833.1. Sequence problems.
X94106 Genomic DNA. Translation: CAA63833.1. Sequence problems.
U24271 Genomic DNA. Translation: AAC99805.1.
BK006941 Genomic DNA. Translation: DAA07984.1.
PIRS64136.
RefSeqNP_011390.2. NM_001180990.1.

3D structure databases

ProteinModelPortalP53128.
SMRP53128. Positions 1-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33126. 22 interactions.
DIPDIP-5188N.
IntActP53128. 2 interactions.
MINTMINT-478501.

Proteomic databases

PaxDbP53128.
PeptideAtlasP53128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL125W; YGL125W; YGL125W.
GeneID852752.
KEGGsce:YGL125W.

Organism-specific databases

CYGDYGL125w.
SGDS000003093. MET13.

Phylogenomic databases

eggNOGCOG0685.
GeneTreeENSGT00390000012490.
HOGENOMHOG000246234.
KOK00297.
OMAYLEFFVS.
OrthoDBEOG7M0P15.

Enzyme and pathway databases

BioCycYEAST:YGL125W-MONOMER.
BRENDA1.5.1.20. 984.
UniPathwayUPA00193.

Gene expression databases

GenevestigatorP53128.

Family and domain databases

InterProIPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamPF02219. MTHFR. 1 hit.
[Graphical view]
TIGRFAMsTIGR00677. fadh2_euk. 1 hit.
ProtoNetSearch...

Other

NextBio972186.
PROP53128.

Entry information

Entry nameMTHR2_YEAST
AccessionPrimary (citable) accession number: P53128
Secondary accession number(s): D6VU23, O94090, Q92318
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 116 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 VII

Yeast (Saccharomyces cerevisiae) chromosome VII: 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