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UniProtKB/Swiss-Prot entry P53128


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTHR2_YEAST
Primary accession number P53128
Secondary accession numbers O94090 Q92318
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 17, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name Methylenetetrahydrofolate reductase 2
Synonyms EC 1.5.1.20
YmL45
Gene name
Name: MET13
Synonyms: MET11, MRPL45
OrderedLocusNames: YGL125W
ORFNames: G2882
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1047::AID-YEA991>3.3.CO;2-E; PubMed=8896269 [NCBI, ExPASy, EBI, Israel, Japan]
Tizon B., Rodriguez-Torres A.M., Rodriguez-Belmonte E., Cadahia J.L., Cerdan E.;
"Identification of a putative methylenetetrahydrofolate reductase by sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII.";
Yeast 12:1047-1051(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
PROTEIN SEQUENCE OF 39-49.
PubMed=9151978 [NCBI, ExPASy, EBI, Israel, Japan]
Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S., Herfurth E., Wittmann-Liebold B., Nishimura T., Isono K.;
"Identification and characterization of the genes for mitochondrial ribosomal proteins of Saccharomyces cerevisiae.";
Eur. J. Biochem. 245:449-456(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-286.
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
Housen I., Lafontaine D., Belot N., Vandenhaute J.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
DOI=10.1006/abbi.1999.1498; PubMed=10600168 [NCBI, ExPASy, EBI, Israel, Japan]
Raymond R.K., Kastanos E.K., Appling D.R.;
"Saccharomyces cerevisiae expresses two genes encoding isozymes of methylenetetrahydrofolate reductase.";
Arch. Biochem. Biophys. 372:300-308(1999).
[6]
FUNCTION.
DOI=10.1074/jbc.M110651200; PubMed=11729203 [NCBI, ExPASy, EBI, Israel, Japan]
Roje S., Chan S.Y., Kaplan F., Raymond R.K., Horne D.W., Appling D.R., Hanson A.D.;
"Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo.";
J. Biol. Chem. 277:4056-4061(2002).
[7]
ERRATUM, AND SEQUENCE REVISION TO 176-181; 197-198 AND 230.
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).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z72647; CAA96833.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94106; CAA63833.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U24271; AAC99805.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64136; S64136.
RefSeq NP_011390.2; -.
3D structure databases
HSSP P00394; 1B5T. [HSSP ENTRY / PDB]
ModBase P53128.
Protein-protein interaction databases
DIP DIP:5188N; -.
IntAct P53128; -.
Organism-specific databases
CYGD YGL125w; -.
SGD S000003093; MET13.
Yeast-GFP YGL125W.
Gene expression databases
ArrayExpress P53128; -.
GermOnline YGL125W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005762; Cellular component: mitochondrial large ribosomal subunit (inferred from direct assay from SGD).
GO:0004489; Molecular function: methylenetetrahydrofolate reductase (NADPH) activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003735; Molecular function: structural constituent of ribosome (inferred from direct assay from SGD).
GO:0006555; Biological process: methionine metabolic process (inferred from mutant phenotype from SGD).
GO:0000097; Biological process: sulfur amino acid biosynthetic process (traceable author statement from SGD).
GO:0006412; Biological process: translation (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR004621; Fadh2_euk.
IPR003171; Mehydrof_redctse.
Graphical view of domain structure.
Pfam PF02219; MTHFR; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00677; fadh2_euk; 1.
BLOCKS P53128.
Proteomic databases
PeptideAtlas P53128; -.
Genome annotation databases
Ensembl YGL125W; Saccharomyces cerevisiae. [Contig view]
GeneID 852752; -.
GenomeReviews Y13135_GR; YGL125W.
KEGG sce:YGL125W; -.
NMPDR fig|4932.3.peg.2494; -.
Phylogenomic databases
HOGENOM P53128; -.
Other
LinkHub P53128; -.
ProtoNet P53128.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   600  600     Methylenetetrahydrofolate reductase 2. PRO_0000190256
CONFLICT   41    42        RM -> LA (in Ref. 3; AA sequence). 
CONFLICT   48    48        P -> A (in Ref. 3; AA sequence). 
CONFLICT   73    73        A -> R (in Ref. 1; CAA63833). 
CONFLICT   152   154        GVA -> RC (in Ref. 4; AAC99805). 
CONFLICT   183   183        Missing (in Ref. 4; AAC99805). 
CONFLICT   211   211        V -> L (in Ref. 4; AAC99805). 
CONFLICT   233   243        GQISIPQHFSS -> ANLHPSTFLV (in Ref. 4; AAC99805). 
CONFLICT   266   276        MCQKLLDSGYV -> CVKIARQWLR (in Ref. 4; AAC99805). 
Sequence information
Length: 600 AA [This is the length of the unprocessed precursor] Molecular weight: 68560 Da [This is the MW of the unprocessed precursor] CRC64: 470B0EFE4E2D1D75 [This is a checksum on the sequence]
        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 

P53128 in FASTA format

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View entry in raw text format (no links)
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