P46151 (MTHR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylenetetrahydrofolate reductase 1
EC=1.5.1.20

Gene names

Name:	MET12
Ordered Locus Names:	YPL023C
ORF Names:	LPB8C

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	657 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.
Sequence similarities	Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	methionine metabolic process Inferred from electronic annotation. Source: InterPro tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	methylenetetrahydrofolate reductase (NADPH) activity Inferred from direct assay PubMed 10600168. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MET13	P53128	2	EBI-11567,EBI-11572

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 657	657	Methylenetetrahydrofolate reductase 1		PRO_0000190255
Amino acid modifications
	Modified residue	120	1	Phosphoserine Ref.7
	Modified residue	301	1	Phosphoserine Ref.7
	Modified residue	358	1	Phosphoserine Ref.6 Ref.7
	Modified residue	359	1	Phosphoserine Ref.6 Ref.7
	Modified residue	407	1	Phosphothreonine Ref.7
Experimental info
	Sequence conflict	110 – 111	2	DP → NL in K02070. Ref.3
	Sequence conflict	115 – 116	2	ED → VV in K02070. Ref.3
	Sequence conflict	119	1	D → V in K02070. Ref.3
	Sequence conflict	124 – 131	8	ESPFKYAV → RLLNMRLF in K02070. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P46151 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: D75612EA92D67500	FASTA	657	73,942
	10 20 30 40 50 60 MSIRDLYHAR ASPFISLEFF PPKTELGTRN LMERMHRMTA LDPLFITVTW GAGGTTAEKT 70 80 90 100 110 120 LTLASLAQQT LNIPVCMHLT CTNTEKAIID DALDRCYNAG IRNILALRGD PPIGEDWLDS 130 140 150 160 170 180 QSNESPFKYA VDLVRYIKQS YGDKFCVGVA AYPEGHCEGE AEGHEQDPLK DLVYLKEKVE 190 200 210 220 230 240 AGADFVITQL FYDVEKFLTF EMLFRERISQ DLPLFPGLMP INSYLLFHRA AKLSHASIPP 250 260 270 280 290 300 AILSRFPPEI QSDDNAVKSI GVDILIELIQ EIYQRTSGRI KGFHFYTLNL EKAIAQIVSQ 310 320 330 340 350 360 SPVLSHIVNE SSEEEGEDET SGEIGSIENV PIEDADGDIV LDDSNEETVA NRKRRRHSSL 370 380 390 400 410 420 DSAKLIFNRA IVTEKGLRYN NENGSMPSKK ALISISKGHG TLGRDATWDE FPNGRFGDSR 430 440 450 460 470 480 SPAYGEIDGY GPSIKVSKSK ALELWGIPKT IGDLKDIFIK YLEGSTDAIP WSDLGLSAET 490 500 510 520 530 540 ALIQEELIQL NYRGYLTLAS QPATNATLSS DKIFGWGPAK GRLYQKAFVE MFIHRQQWET 550 560 570 580 590 600 TLKPKLDHYG RRKFSYYAGD SSGSFETNLD PHSSSVVTWG VFPNSPVKQT TIIEEESFKA 610 620 630 640 650 WRDEAFSIWS EWAKLFPRNT PANILLRLVH KDYCLVSIVH HDFKETDELW EMLLDQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Molecular cloning and nucleotide sequence analysis of the Saccharomyces cerevisiae RAD1 gene." Yang E., Friedberg E.C. Mol. Cell. Biol. 4:2161-2169(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
[4]	"Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification." Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S., Matthews R.G., Rozen R. Nat. Genet. 7:195-200(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[5]	Erratum Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S., Matthews R.G., Rozen R. Nat. Genet. 7:551-551(1994) [PubMed] [Europe PMC] [Abstract]
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-359, MASS SPECTROMETRY.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-301; SER-358; SER-359 AND THR-407, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U36624 Genomic DNA. Translation: AAB68164.1. K02070 Genomic DNA. No translation available. BK006949 Genomic DNA. Translation: DAA11405.1.
PIR	S63459.
RefSeq	NP_015302.1. NM_001183837.1.
3D structure databases
ProteinModelPortal	P46151.
SMR	P46151. Positions 1-300.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2825N.
IntAct	P46151. 5 interactions.
MINT	MINT-1699985.
STRING	4932.YPL023C.
Proteomic databases
PaxDb	P46151.
PeptideAtlas	P46151.
PRIDE	P46151.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPL023C; YPL023C; YPL023C.
GeneID	856084.
KEGG	sce:YPL023C.
Organism-specific databases
CYGD	YPL023c.
SGD	S000005944. MET12.
Phylogenomic databases
eggNOG	COG0685.
GeneTree	ENSGT00650000094052.
HOGENOM	HOG000246234.
KO	K00297.
OMA	YGEIDGY.
OrthoDB	EOG444PTG.
Enzyme and pathway databases
BioCyc	YEAST:YPL023C-MONOMER.
UniPathway	UPA00193.
Gene expression databases
Genevestigator	P46151.
GermOnline	YPL023C. 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	981098.

Entry information

Entry name

MTHR1_YEAST

Accession

Primary (citable) accession number: P46151
Secondary accession number(s): D6W3Y9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program