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Q10258 (MTHR1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylenetetrahydrofolate reductase 1

EC=1.5.1.20
Gene names
Name:met9
ORF Names:SPAC56F8.10
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion.

Disruption phenotype

Leads to strict auxotrophy for methionine. Ref.1

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Methylenetetrahydrofolate reductase 1
PRO_0000190253

Regions

Nucleotide binding21 – 266NAD By similarity
Nucleotide binding53 – 542NAD and FAD By similarity
Nucleotide binding112 – 1143FAD By similarity
Nucleotide binding130 – 1312FAD By similarity

Sites

Active site211Proton donor/acceptor By similarity
Binding site821FAD By similarity
Binding site1141Substrate By similarity
Binding site1531FAD By similarity
Binding site1731FAD By similarity
Binding site1841Substrate By similarity
Binding site2761Substrate By similarity

Amino acid modifications

Modified residue3551Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q10258 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 38519FEE783D331F

FASTA60369,012
        10         20         30         40         50         60 
MKISDKLLHP DWKEKVTYSY EFFPPKTSTG VQNLYNRIDR MKTWGRPMFV DVTWGAGGTS 

        70         80         90        100        110        120 
SELTPGIVNV IQTDFEVDTC MHLTCTNMST EMIDAALKRA HETGCRNILA LRGDPVKDTD 

       130        140        150        160        170        180 
WTEGESGFRY ASDLVRYIRT HYNDEFCIGV AGYPEGYSPD DDIDESIKHL KLKVDEGADF 

       190        200        210        220        230        240 
IVTQMFYDVD NFIAWVDKVR AAGINIPIFP GIMPIQAWDS FIRRAKWSGV KIPQHFMDTL 

       250        260        270        280        290        300 
VPVKDDDEGV RERGVELIVE MCRKLIASGI TRLHFYTMNL EKAVKMIIER LGLLDENLAP 

       310        320        330        340        350        360 
IVDTNNVELT NASSQDRRIN EGVRPIFWRT RNESYVSRTD QWDELPHGRW GDSRSPAFGE 

       370        380        390        400        410        420 
FDAIRYGLRM SPKEITTSWG SPKSYSEIGD LFARYCEKKI SSLPWSDLPI SDEADLIRDQ 

       430        440        450        460        470        480 
LLSMNRNAFL TINSQPALNG EKSSHPVFGW GPPNGYVFQK PYVEFFVHPS LLNELKETVK 

       490        500        510        520        530        540 
KLNSVSYFVT NKNGDLDTNS QYEIPNAVTW GVFPNREIIQ PTIVESTSFL AWKDEAYSLG 

       550        560        570        580        590        600 
MEWANAYSPD SISRKLLVSM MKEWFLCVIV DNDFQNGQSL FDVFNKMRSL KDIHPELYYA 


NAS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA93581.1.
PIRT38920.
RefSeqNP_593224.1. NM_001018621.2.

3D structure databases

ProteinModelPortalQ10258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279431. 1 interaction.
MINTMINT-4698197.
STRING4896.SPAC56F8.10-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC56F8.10.1; SPAC56F8.10.1:pep; SPAC56F8.10.
GeneID2542993.
KEGGspo:SPAC56F8.10.

Organism-specific databases

PomBaseSPAC56F8.10.

Phylogenomic databases

eggNOGCOG0685.
HOGENOMHOG000246234.
KOK00297.
OMAYLEFFVS.
OrthoDBEOG7M0P15.
PhylomeDBQ10258.

Enzyme and pathway databases

UniPathwayUPA00193.

Family and domain databases

InterProIPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamPF02219. MTHFR. 1 hit.
[Graphical view]
TIGRFAMsTIGR00677. fadh2_euk. 1 hit.
ProtoNetSearch...

Other

NextBio20804026.
PROQ10258.

Entry information

Entry nameMTHR1_SCHPO
AccessionPrimary (citable) accession number: Q10258
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways