P53128 (MTHR2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylenetetrahydrofolate reductase 2
EC=1.5.1.20

Alternative name(s):
YmL45

Gene names

Name:	MET13
Synonyms:	MET11, MRPL45
Ordered Locus Names:	YGL125W
ORF Names:	G2882

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	600 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.
Cofactor	FAD By similarity.
Pathway	One-carbon metabolism; tetrahydrofolate interconversion.
Miscellaneous	Present with 8600 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the methylenetetrahydrofolate reductase family.
Caution	Was originally (Ref.4) thought to be a mitochondrial ribosomal protein.
Sequence caution	The sequence CAA63833.1 differs from that shown. Reason: Sequencing errors. The sequence CAA96833.1 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	methionine biosynthetic process Inferred from mutant phenotype PubMed 10029993Ref.6. Source: SGD tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD
Molecular_function	methylenetetrahydrofolate reductase (NADPH) activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MET12	P46151	2	EBI-11572,EBI-11567

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 600	600	Methylenetetrahydrofolate reductase 2		PRO_0000190256
Experimental info
	Sequence conflict	41 – 42	2	RM → LA AA sequence Ref.4
	Sequence conflict	48	1	P → A AA sequence Ref.4
	Sequence conflict	73	1	A → R in CAA63833. Ref.1
	Sequence conflict	152 – 154	3	GVA → RC in AAC99805. Ref.5
	Sequence conflict	183	1	Missing in AAC99805. Ref.5
	Sequence conflict	211	1	V → L in AAC99805. Ref.5
	Sequence conflict	233 – 243	11	GQISIPQHFSS → ANLHPSTFLV in AAC99805. Ref.5
	Sequence conflict	266 – 276	11	MCQKLLDSGYV → CVKIARQWLR in AAC99805. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P53128 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 470B0EFE4E2D1D75	FASTA	600	68,560
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S64136.
RefSeq	NP_011390.2. NM_001180990.1.
3D structure databases
ProteinModelPortal	P53128.
SMR	P53128. Positions 1-301.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5188N.
IntAct	P53128. 2 interactions.
MINT	MINT-478501.
Proteomic databases
PaxDb	P53128.
PeptideAtlas	P53128.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL125W; YGL125W; YGL125W.
GeneID	852752.
KEGG	sce:YGL125W.
Organism-specific databases
CYGD	YGL125w.
SGD	S000003093. MET13.
Phylogenomic databases
eggNOG	COG0685.
GeneTree	ENSGT00390000012490.
HOGENOM	HOG000246234.
KO	K00297.
OMA	VVGWGPS.
OrthoDB	EOG46HKK5.
Enzyme and pathway databases
BioCyc	YEAST:YGL125W-MONOMER.
BRENDA	1.5.1.20. 984.
UniPathway	UPA00193.
Gene expression databases
Genevestigator	P53128.
GermOnline	YGL125W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004621. Fadh2_euk. IPR003171. Mehydrof_redctse. [Graphical view]
Pfam	PF02219. MTHFR. 1 hit. [Graphical view]
TIGRFAMs	TIGR00677. fadh2_euk. 1 hit.
ProtoNet	Search...
Other
NextBio	972186.

Entry information

Entry name

MTHR2_YEAST

Accession

Primary (citable) accession number: P53128
Secondary accession number(s): D6VU23, O94090, Q92318

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program