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Reviewed, UniProtKB/Swiss-Prot P53128 (MTHR2_YEAST)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 pathway.

Miscellaneous

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

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Caution

Was originally (Ref.3) thought to be a mitochondrial ribosomal protein.

Sequence caution

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

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MET12P461511EBI-11572,EBI-11567

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 600600Methylenetetrahydrofolate reductase 2
PRO_0000190256

Experimental info

Sequence conflict41 – 422RM → LA AA sequence Ref.3
Sequence conflict481P → A AA sequence Ref.3
Sequence conflict731A → R in CAA63833. Ref.1
Sequence conflict152 – 1543GVA → RC in AAC99805. Ref.4
Sequence conflict1831Missing in AAC99805. Ref.4
Sequence conflict2111V → L in AAC99805. Ref.4
Sequence conflict233 – 24311GQISIPQHFSS → ANLHPSTFLV in AAC99805. Ref.4
Sequence conflict266 – 27611MCQKLLDSGYV → CVKIARQWLR in AAC99805. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P53128-1 [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: 8896269] [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: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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: 9151978] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-49.
[4]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.
[5]"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: 10600168] [Abstract]
Cited for: FUNCTION.
[6]"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: 11729203] [Abstract]
Cited for: FUNCTION.
[7]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.
[8]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

Z72647 Genomic DNA. Translation: CAA96833.1. Sequence problems.
X94106 Genomic DNA. Translation: CAA63833.1. Sequence problems.
U24271 Genomic DNA. Translation: AAC99805.1.
PIRS64136.
RefSeqNP_011390.2.

3D structure databases

HSSPHSSP built from PDB template 1B5T based on UniProtKB P00394.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5188N.
IntActP53128.

Proteomic databases

PeptideAtlasP53128.

Genome annotation databases

EnsemblYGL125W. Saccharomyces cerevisiae. [Contig view]
GeneID852752.
GenomeReviewsGene locus YGL125W in contig Y13135_GR.
KEGGsce:YGL125W.
NMPDRfig|4932.3.peg.2494.

Organism-specific databases

CYGDYGL125w.
SGDS000003093. MET13.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP53128.

Gene expression databases

ArrayExpressP53128.
GermOnlineYGL125W. Saccharomyces cerevisiae.

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 Resources

LinkHubP53128.
NextBio972186.

Entry information

Entry nameMTHR2_YEAST
AccessionPrimary (citable) accession number: P53128
Secondary accession number(s): O94090, Q92318
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: November 25, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents