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P53128

- MTHR2_YEAST

UniProt

P53128 - MTHR2_YEAST

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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

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

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. 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 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. 23 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.
InParanoidi P53128.
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: October 29, 2014
This is version 120 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