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Protein

Methylenetetrahydrofolate reductase 1

Gene

met9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. Performs 80 to 85 percent of the total methylenetetrahydrofolate reductase activity of the cells.1 Publication

Catalytic activityi

5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.1 Publication

Cofactori

FADBy similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei21 – 211Proton donor/acceptorBy similarity
Binding sitei82 – 821FADBy similarity
Binding sitei114 – 1141SubstrateBy similarity
Binding sitei153 – 1531FADBy similarity
Binding sitei173 – 1731FADBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei276 – 2761SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 266NADBy similarity
Nucleotide bindingi53 – 542NAD and FADBy similarity
Nucleotide bindingi112 – 1143FADBy similarity
Nucleotide bindingi130 – 1312FADBy similarity

GO - Molecular functioni

  • methylenetetrahydrofolate reductase (NAD(P)H) activity Source: PomBase

GO - Biological processi

  • methionine biosynthetic process Source: PomBase
  • one-carbon metabolic process Source: GO_Central
  • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.5.1.20. 5613.
ReactomeiREACT_333030. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylenetetrahydrofolate reductase 1 (EC:1.5.1.20)
Gene namesi
Name:met9
ORF Names:SPAC56F8.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC56F8.10.
PomBaseiSPAC56F8.10.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Leads to strict auxotrophy for methionine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Methylenetetrahydrofolate reductase 1PRO_0000190253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei355 – 3551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10258.

Interactioni

Protein-protein interaction databases

MINTiMINT-4698197.
STRINGi4896.SPAC56F8.10-1.

Structurei

3D structure databases

ProteinModelPortaliQ10258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000246234.
InParanoidiQ10258.
KOiK00297.
OMAiYLEFFVS.
OrthoDBiEOG7M0P15.
PhylomeDBiQ10258.

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.

Q10258-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKISDKLLHP DWKEKVTYSY EFFPPKTSTG VQNLYNRIDR MKTWGRPMFV
60 70 80 90 100
DVTWGAGGTS SELTPGIVNV IQTDFEVDTC MHLTCTNMST EMIDAALKRA
110 120 130 140 150
HETGCRNILA LRGDPVKDTD WTEGESGFRY ASDLVRYIRT HYNDEFCIGV
160 170 180 190 200
AGYPEGYSPD DDIDESIKHL KLKVDEGADF IVTQMFYDVD NFIAWVDKVR
210 220 230 240 250
AAGINIPIFP GIMPIQAWDS FIRRAKWSGV KIPQHFMDTL VPVKDDDEGV
260 270 280 290 300
RERGVELIVE MCRKLIASGI TRLHFYTMNL EKAVKMIIER LGLLDENLAP
310 320 330 340 350
IVDTNNVELT NASSQDRRIN EGVRPIFWRT RNESYVSRTD QWDELPHGRW
360 370 380 390 400
GDSRSPAFGE FDAIRYGLRM SPKEITTSWG SPKSYSEIGD LFARYCEKKI
410 420 430 440 450
SSLPWSDLPI SDEADLIRDQ LLSMNRNAFL TINSQPALNG EKSSHPVFGW
460 470 480 490 500
GPPNGYVFQK PYVEFFVHPS LLNELKETVK KLNSVSYFVT NKNGDLDTNS
510 520 530 540 550
QYEIPNAVTW GVFPNREIIQ PTIVESTSFL AWKDEAYSLG MEWANAYSPD
560 570 580 590 600
SISRKLLVSM MKEWFLCVIV DNDFQNGQSL FDVFNKMRSL KDIHPELYYA

NAS
Length:603
Mass (Da):69,012
Last modified:October 1, 1996 - v1
Checksum:i38519FEE783D331F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93581.1.
PIRiT38920.
RefSeqiNP_593224.1. NM_001018621.2.

Genome annotation databases

EnsemblFungiiSPAC56F8.10.1; SPAC56F8.10.1:pep; SPAC56F8.10.
GeneIDi2542993.
KEGGispo:SPAC56F8.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93581.1.
PIRiT38920.
RefSeqiNP_593224.1. NM_001018621.2.

3D structure databases

ProteinModelPortaliQ10258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4698197.
STRINGi4896.SPAC56F8.10-1.

Proteomic databases

MaxQBiQ10258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC56F8.10.1; SPAC56F8.10.1:pep; SPAC56F8.10.
GeneIDi2542993.
KEGGispo:SPAC56F8.10.

Organism-specific databases

EuPathDBiFungiDB:SPAC56F8.10.
PomBaseiSPAC56F8.10.

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000246234.
InParanoidiQ10258.
KOiK00297.
OMAiYLEFFVS.
OrthoDBiEOG7M0P15.
PhylomeDBiQ10258.

Enzyme and pathway databases

UniPathwayiUPA00193.
BRENDAi1.5.1.20. 5613.
ReactomeiREACT_333030. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi20804026.
PROiQ10258.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two non-complementing genes encoding enzymatically active methylenetetrahydrofolate reductases control methionine requirement in fission yeast Schizosaccharomyces pombe."
    Naula N., Walther C., Baumann D., Schweingruber M.E.
    Yeast 19:841-848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMTHR1_SCHPO
AccessioniPrimary (citable) accession number: Q10258
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 27, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.