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P53128

- MTHR2_YEAST

UniProt

P53128 - MTHR2_YEAST

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Protein

Methylenetetrahydrofolate reductase 2

Gene
MET13, MET11, MRPL45, YGL125W, G2882
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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/acceptor By similarity
Binding sitei84 – 841FAD By similarity
Binding sitei116 – 1161Substrate By similarity
Binding sitei156 – 1561FAD By similarity
Binding sitei171 – 1711FAD By similarity
Binding sitei178 – 1781FAD By similarity
Binding sitei189 – 1891Substrate By similarity
Binding sitei282 – 2821Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 276NAD By similarity
Nucleotide bindingi54 – 552NAD and FAD By similarity
Nucleotide bindingi114 – 1163FAD By similarity
Nucleotide bindingi133 – 1342FAD By 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
Complete GO annotation...

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.

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.

Sequence conflict

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 118 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.

Caution

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

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

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