ID   MTHR2_YEAST             Reviewed;         600 AA.
AC   P53128; O94090; Q92318;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Methylenetetrahydrofolate reductase 2;
DE            EC=1.5.1.20;
DE   AltName: Full=YmL45;
GN   Name=MET13; Synonyms=MET11, MRPL45; OrderedLocusNames=YGL125W;
GN   ORFNames=G2882;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97051592; PubMed=8896269;
RX   DOI=10.1002/(SICI)1097-0061(199609)12:10B<1047::AID-YEA991>3.3.CO;2-E;
RA   Tizon B., Rodriguez-Torres A.M., Rodriguez-Belmonte E., Cadahia J.L.,
RA   Cerdan E.;
RT   "Identification of a putative methylenetetrahydrofolate reductase by
RT   sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII.";
RL   Yeast 12:1047-1051(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313265; PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 39-49.
RX   MEDLINE=97296414; PubMed=9151978;
RX   DOI=10.1111/j.1432-1033.1997.t01-2-00449.x;
RA   Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S.,
RA   Herfurth E., Wittmann-Liebold B., Nishimura T., Isono K.;
RT   "Identification and characterization of the genes for mitochondrial
RT   ribosomal proteins of Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 245:449-456(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-286.
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RA   Housen I., Lafontaine D., Belot N., Vandenhaute J.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   PubMed=10600168; DOI=10.1006/abbi.1999.1498;
RA   Raymond R.K., Kastanos E.K., Appling D.R.;
RT   "Saccharomyces cerevisiae expresses two genes encoding isozymes of
RT   methylenetetrahydrofolate reductase.";
RL   Arch. Biochem. Biophys. 372:300-308(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=11729203; DOI=10.1074/jbc.M110651200;
RA   Roje S., Chan S.Y., Kaplan F., Raymond R.K., Horne D.W., Appling D.R.,
RA   Hanson A.D.;
RT   "Metabolic engineering in yeast demonstrates that S-adenosylmethionine
RT   controls flux through the methylenetetrahydrofolate reductase reaction
RT   in vivo.";
RL   J. Biol. Chem. 277:4056-4061(2002).
RN   [7]
RP   ERRATUM, AND SEQUENCE REVISION TO 176-181; 197-198 AND 230.
RA   Roje S., Chan S.Y., Kaplan F., Raymond R.K., Horne D.W., Appling D.R.,
RA   Hanson A.D.;
RL   J. Biol. Chem. 277:36904-36904(2002).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10-
CC       methylenetetrahydrofolate + NAD(P)H.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- INTERACTION:
CC       P38009:ADE17; NbExp=1; IntAct=EBI-11572, EBI-14223;
CC       P32324:EFT1; NbExp=1; IntAct=EBI-11572, EBI-6333;
CC       P11986:INO1; NbExp=1; IntAct=EBI-11572, EBI-9257;
CC       P46151:MET12; NbExp=1; IntAct=EBI-11572, EBI-11567;
CC       P41940:MPG1; NbExp=1; IntAct=EBI-11572, EBI-11191;
CC       P25293:NAP1; NbExp=1; IntAct=EBI-11572, EBI-11850;
CC       P37012:PGM2; NbExp=1; IntAct=EBI-11572, EBI-13296;
CC       Q04383:PLM2; NbExp=1; IntAct=EBI-11572, EBI-2079237;
CC       P28274:URA7; NbExp=1; IntAct=EBI-11572, EBI-20128;
CC   -!- MISCELLANEOUS: Present with 8600 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase
CC       family.
CC   -!- CAUTION: Was originally (PubMed:9151978) thought to be a
CC       mitochondrial ribosomal protein.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA63833.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC       Sequence=CAA96833.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
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DR   EMBL; Z72647; CAA96833.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X94106; CAA63833.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U24271; AAC99805.1; -; Genomic_DNA.
DR   PIR; S64136; S64136.
DR   RefSeq; NP_011390.2; -.
DR   HSSP; P00394; 1B5T.
DR   DIP; DIP:5188N; -.
DR   IntAct; P53128; 15.
DR   PeptideAtlas; P53128; -.
DR   Ensembl; YGL125W; Saccharomyces cerevisiae.
DR   GeneID; 852752; -.
DR   GenomeReviews; Y13135_GR; YGL125W.
DR   KEGG; sce:YGL125W; -.
DR   NMPDR; fig|4932.3.peg.2494; -.
DR   CYGD; YGL125w; -.
DR   SGD; S000003093; MET13.
DR   HOGENOM; P53128; -.
DR   OMA; P53128; DITWHPA.
DR   BRENDA; 1.5.1.20; 250.
DR   NextBio; 972186; -.
DR   ArrayExpress; P53128; -.
DR   GermOnline; YGL125W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NADPH)...; IDA:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0009086; P:methionine biosynthetic process; IMP:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004621; Fadh2_euk.
DR   InterPro; IPR003171; Mehydrof_redctse.
DR   Pfam; PF02219; MTHFR; 1.
DR   TIGRFAMs; TIGR00677; fadh2_euk; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    600       Methylenetetrahydrofolate reductase 2.
FT                                /FTId=PRO_0000190256.
FT   CONFLICT     41     42       RM -> LA (in Ref. 3; AA sequence).
FT   CONFLICT     48     48       P -> A (in Ref. 3; AA sequence).
FT   CONFLICT     73     73       A -> R (in Ref. 1; CAA63833).
FT   CONFLICT    152    154       GVA -> RC (in Ref. 4; AAC99805).
FT   CONFLICT    183    183       Missing (in Ref. 4; AAC99805).
FT   CONFLICT    211    211       V -> L (in Ref. 4; AAC99805).
FT   CONFLICT    233    243       GQISIPQHFSS -> ANLHPSTFLV (in Ref. 4;
FT                                AAC99805).
FT   CONFLICT    266    276       MCQKLLDSGYV -> CVKIARQWLR (in Ref. 4;
FT                                AAC99805).
SQ   SEQUENCE   600 AA;  68560 MW;  470B0EFE4E2D1D75 CRC64;
     MKITEKLEQH RQTSGKPTYS FEYFVPKTTQ GVQNLYDRMD RMYEASLPQF IDITWNAGGG
     RLSHLSTDLV ATAQSVLGLE TCMHLTCTNM PISMIDDALE NAYHSGCQNI LALRGDPPRD
     AENWTPVEGG FQYAKDLIKY IKSKYGDHFA IGVAGYPECH PELPNKDVKL DLEYLKQKID
     AGGDFIITQM FYDVDNFINW CSQVRAAGMD VPIIPGIMPI TTYAAFLRRA QWGQISIPQH
     FSSRLDPIKD DDELVRDIGT NLIVEMCQKL LDSGYVSHLH IYTMNLEKAP LMILERLNIL
     PTESEFNAHP LAVLPWRKSL NPKRKNEEVR PIFWKRRPYS YVARTSQWAV DEFPNGRFGD
     SSSPAFGDLD LCGSDLIRQS ANKCLELWST PTSINDVAFL VINYLNGNLK CLPWSDIPIN
     DEINPIKAHL IELNQHSIIT INSQPQVNGI RSNDKIHGWG PKDGYVYQKQ YLEFMLPKTK
     LPKLIDTLKN NEFLTYFAID SQGDLLSNHP DNSKSNAVTW GIFPGREILQ PTIVEKISFL
     AWKEEFYHIL NEWKLNMNKY DKPHSAQFIQ SLIDDYCLVN IVDNDYISPD DQIHSILLSL
//