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Protein

Methylenetetrahydrofolate reductase 2

Gene

MET13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

FADBy 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

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.
ReactomeiREACT_324954. Metabolism of folate and pterines.
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 Componenti: 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. 23 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.
InParanoidiP53128.
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

        10         20         30         40         50
MKITEKLEQH RQTSGKPTYS FEYFVPKTTQ GVQNLYDRMD RMYEASLPQF
60 70 80 90 100
IDITWNAGGG RLSHLSTDLV ATAQSVLGLE TCMHLTCTNM PISMIDDALE
110 120 130 140 150
NAYHSGCQNI LALRGDPPRD AENWTPVEGG FQYAKDLIKY IKSKYGDHFA
160 170 180 190 200
IGVAGYPECH PELPNKDVKL DLEYLKQKID AGGDFIITQM FYDVDNFINW
210 220 230 240 250
CSQVRAAGMD VPIIPGIMPI TTYAAFLRRA QWGQISIPQH FSSRLDPIKD
260 270 280 290 300
DDELVRDIGT NLIVEMCQKL LDSGYVSHLH IYTMNLEKAP LMILERLNIL
310 320 330 340 350
PTESEFNAHP LAVLPWRKSL NPKRKNEEVR PIFWKRRPYS YVARTSQWAV
360 370 380 390 400
DEFPNGRFGD SSSPAFGDLD LCGSDLIRQS ANKCLELWST PTSINDVAFL
410 420 430 440 450
VINYLNGNLK CLPWSDIPIN DEINPIKAHL IELNQHSIIT INSQPQVNGI
460 470 480 490 500
RSNDKIHGWG PKDGYVYQKQ YLEFMLPKTK LPKLIDTLKN NEFLTYFAID
510 520 530 540 550
SQGDLLSNHP DNSKSNAVTW GIFPGREILQ PTIVEKISFL AWKEEFYHIL
560 570 580 590 600
NEWKLNMNKY DKPHSAQFIQ SLIDDYCLVN IVDNDYISPD DQIHSILLSL
Length:600
Mass (Da):68,560
Last modified:October 16, 2006 - v2
Checksum:i470B0EFE4E2D1D75
GO

Sequence cautioni

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

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 (Ref. 5) Curated
Sequence conflicti183 – 1831Missing in AAC99805 (Ref. 5) Curated
Sequence conflicti211 – 2111V → L in AAC99805 (Ref. 5) Curated
Sequence conflicti233 – 24311GQISIPQHFSS → ANLHPSTFLV in AAC99805 (Ref. 5) CuratedAdd
BLAST
Sequence conflicti266 – 27611MCQKLLDSGYV → CVKIARQWLR in AAC99805 (Ref. 5) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi33126. 23 interactions.
DIPiDIP-5188N.
IntActiP53128. 2 interactions.
MINTiMINT-478501.

Proteomic databases

MaxQBiP53128.
PaxDbiP53128.
PeptideAtlasiP53128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYGL125w.
SGDiS000003093. MET13.

Phylogenomic databases

eggNOGiCOG0685.
GeneTreeiENSGT00390000012490.
HOGENOMiHOG000246234.
InParanoidiP53128.
KOiK00297.
OMAiYLEFFVS.
OrthoDBiEOG7M0P15.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciYEAST:YGL125W-MONOMER.
BRENDAi1.5.1.20. 984.
ReactomeiREACT_324954. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi972186.
PROiP53128.

Gene expression databases

GenevestigatoriP53128.

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.
ProtoNetiSearch...

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(1995) [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(1996) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-49.
  5. Housen I., Lafontaine D., Belot N., Vandenhaute J.
    Submitted (MAR-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(1998) [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(2001) [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(2001)
    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: September 30, 1996
Last sequence update: October 16, 2006
Last modified: March 31, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.