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P53128

- MTHR2_YEAST

UniProt

P53128 - MTHR2_YEAST

Protein

Methylenetetrahydrofolate reductase 2

Gene

MET13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei22 – 221Proton donor/acceptorBy similarity
    Binding sitei84 – 841FADBy similarity
    Binding sitei116 – 1161SubstrateBy similarity
    Binding sitei156 – 1561FADBy similarity
    Binding sitei171 – 1711FADBy similarity
    Binding sitei178 – 1781FADBy similarity
    Binding sitei189 – 1891SubstrateBy similarity
    Binding sitei282 – 2821SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 276NADBy similarity
    Nucleotide bindingi54 – 552NAD and FADBy similarity
    Nucleotide bindingi114 – 1163FADBy similarity
    Nucleotide bindingi133 – 1342FADBy similarity

    GO - Molecular functioni

    1. methylenetetrahydrofolate reductase (NAD(P)H) activity Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. methionine biosynthetic process Source: SGD
    2. tetrahydrofolate interconversion Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciYEAST:YGL125W-MONOMER.
    BRENDAi1.5.1.20. 984.
    UniPathwayiUPA00193.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylenetetrahydrofolate reductase 2 (EC:1.5.1.20)
    Alternative name(s):
    YmL45
    Gene namesi
    Name:MET13
    Synonyms:MET11, MRPL45
    Ordered Locus Names:YGL125W
    ORF Names:G2882
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL125w.
    SGDiS000003093. MET13.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 600600Methylenetetrahydrofolate reductase 2PRO_0000190256Add
    BLAST

    Proteomic databases

    MaxQBiP53128.
    PaxDbiP53128.
    PeptideAtlasiP53128.

    Expressioni

    Gene expression databases

    GenevestigatoriP53128.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MET12P461512EBI-11572,EBI-11567

    Protein-protein interaction databases

    BioGridi33126. 22 interactions.
    DIPiDIP-5188N.
    IntActiP53128. 2 interactions.
    MINTiMINT-478501.

    Structurei

    3D structure databases

    ProteinModelPortaliP53128.
    SMRiP53128. Positions 1-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0685.
    GeneTreeiENSGT00390000012490.
    HOGENOMiHOG000246234.
    KOiK00297.
    OMAiYLEFFVS.
    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.

    P53128-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKITEKLEQH RQTSGKPTYS FEYFVPKTTQ GVQNLYDRMD RMYEASLPQF    50
    IDITWNAGGG RLSHLSTDLV ATAQSVLGLE TCMHLTCTNM PISMIDDALE 100
    NAYHSGCQNI LALRGDPPRD AENWTPVEGG FQYAKDLIKY IKSKYGDHFA 150
    IGVAGYPECH PELPNKDVKL DLEYLKQKID AGGDFIITQM FYDVDNFINW 200
    CSQVRAAGMD VPIIPGIMPI TTYAAFLRRA QWGQISIPQH FSSRLDPIKD 250
    DDELVRDIGT NLIVEMCQKL LDSGYVSHLH IYTMNLEKAP LMILERLNIL 300
    PTESEFNAHP LAVLPWRKSL NPKRKNEEVR PIFWKRRPYS YVARTSQWAV 350
    DEFPNGRFGD SSSPAFGDLD LCGSDLIRQS ANKCLELWST PTSINDVAFL 400
    VINYLNGNLK CLPWSDIPIN DEINPIKAHL IELNQHSIIT INSQPQVNGI 450
    RSNDKIHGWG PKDGYVYQKQ YLEFMLPKTK LPKLIDTLKN NEFLTYFAID 500
    SQGDLLSNHP DNSKSNAVTW GIFPGREILQ PTIVEKISFL AWKEEFYHIL 550
    NEWKLNMNKY DKPHSAQFIQ SLIDDYCLVN IVDNDYISPD DQIHSILLSL 600
    Length:600
    Mass (Da):68,560
    Last modified:October 17, 2006 - v2
    Checksum:i470B0EFE4E2D1D75
    GO

    Sequence cautioni

    The sequence CAA63833.1 differs from that shown. Reason: Sequencing errors.
    The sequence CAA96833.1 differs from that shown. Reason: Sequencing errors.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 422RM → LA AA sequence (PubMed:9151978)Curated
    Sequence conflicti48 – 481P → A AA sequence (PubMed:9151978)Curated
    Sequence conflicti73 – 731A → R in CAA63833. (PubMed:8896269)Curated
    Sequence conflicti152 – 1543GVA → RC in AAC99805. 1 PublicationCurated
    Sequence conflicti183 – 1831Missing in AAC99805. 1 PublicationCurated
    Sequence conflicti211 – 2111V → L in AAC99805. 1 PublicationCurated
    Sequence conflicti233 – 24311GQISIPQHFSS → ANLHPSTFLV in AAC99805. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti266 – 27611MCQKLLDSGYV → CVKIARQWLR in AAC99805. 1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS64136.
    RefSeqiNP_011390.2. NM_001180990.1.

    Genome annotation databases

    EnsemblFungiiYGL125W; YGL125W; YGL125W.
    GeneIDi852752.
    KEGGisce:YGL125W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S64136.
    RefSeqi NP_011390.2. NM_001180990.1.

    3D structure databases

    ProteinModelPortali P53128.
    SMRi P53128. Positions 1-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33126. 22 interactions.
    DIPi DIP-5188N.
    IntActi P53128. 2 interactions.
    MINTi MINT-478501.

    Proteomic databases

    MaxQBi P53128.
    PaxDbi P53128.
    PeptideAtlasi P53128.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL125W ; YGL125W ; YGL125W .
    GeneIDi 852752.
    KEGGi sce:YGL125W.

    Organism-specific databases

    CYGDi YGL125w.
    SGDi S000003093. MET13.

    Phylogenomic databases

    eggNOGi COG0685.
    GeneTreei ENSGT00390000012490.
    HOGENOMi HOG000246234.
    KOi K00297.
    OMAi YLEFFVS.
    OrthoDBi EOG7M0P15.

    Enzyme and pathway databases

    UniPathwayi UPA00193 .
    BioCyci YEAST:YGL125W-MONOMER.
    BRENDAi 1.5.1.20. 984.

    Miscellaneous databases

    NextBioi 972186.
    PROi P53128.

    Gene expression databases

    Genevestigatori P53128.

    Family and domain databases

    Gene3Di 3.20.20.220. 1 hit.
    InterProi IPR029041. FAD-linked_oxidoreductase-like.
    IPR004621. Fadh2_euk.
    IPR003171. Mehydrof_redctse.
    [Graphical view ]
    Pfami PF02219. MTHFR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51730. SSF51730. 1 hit.
    TIGRFAMsi TIGR00677. fadh2_euk. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMTHR2_YEAST
    AccessioniPrimary (citable) accession number: P53128
    Secondary accession number(s): D6VU23, O94090, Q92318
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8600 molecules/cell in log phase SD medium.1 Publication

    Caution

    Was originally thought to be a mitochondrial ribosomal protein.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3