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O74927 (MTHR2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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 2

EC=1.5.1.20
Gene names
Name:met11
Synonyms:mthfr2
ORF Names:SPAC343.10
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length641 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 15 to 20 percent of the total methylenetetrahydrofolate reductase activity of the cells.

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 partial auxotrophy for methionine. Ref.1

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 641641Methylenetetrahydrofolate reductase 2
PRO_0000190254

Regions

Nucleotide binding20 – 256NAD By similarity
Nucleotide binding52 – 532NAD and FAD By similarity
Nucleotide binding111 – 1133FAD By similarity

Sites

Active site201Proton donor/acceptor By similarity
Binding site811FAD By similarity
Binding site1131Substrate By similarity
Binding site1531FAD By similarity
Binding site1721FAD By similarity
Binding site1791FAD By similarity
Binding site1901Substrate By similarity

Experimental info

Sequence conflict2021E → D in BAA13780. Ref.3
Sequence conflict2811G → A in BAA13780. Ref.3
Sequence conflict4551A → V in BAA13780. Ref.3
Sequence conflict537 – 641105QVTYY…LEIDF → HVRSNFSSSISDSTCFQRLV SKPLFLRIRATDRSKFSVQK in BAA13780. Ref.3
Sequence conflict6141I → L in CAA09738. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O74927 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: E7AFFDD1F2C1C8A4

FASTA64172,140
        10         20         30         40         50         60 
MKIVDLIDKI PNGNAFYSFE YFPPKTTVGL ENLSSRITRM SRNMMPLFSS VTWGTAGSTA 

        70         80         90        100        110        120 
EVSIYLAKML EQHHKIPACL HLTCTNVDKA IIDKALETAK EYGIRNILAL RGDPPLNSDH 

       130        140        150        160        170        180 
WEGKVSEFEH AVDLVRYIRE KYGDYFCIGV AAYPEGHVDS NVPELSKDPL RDIPFLIEKV 

       190        200        210        220        230        240 
EAGADFIITQ IFYEPEAFIK FENFVRNHSS NALRNIPIIP AIMPIQSYGS LKRMTRLCGC 

       250        260        270        280        290        300 
SVPSSLMQRL NAAKPDDEAI KNIGVEHIVD MIKKIMDNVQ GRVHGFHFCT LNLERSVALI 

       310        320        330        340        350        360 
LKNSGLLTKR WKQVESEMED EKLLRTTRKR LSLDEPAELH NQVVVPSQQP VADKSSNLFV 

       370        380        390        400        410        420 
TSKQSSVSGH KDNLTEEAPF SVSEGSGVLG RQANWDDFTN GRFGDPRSPA YGEIDGYGPT 

       430        440        450        460        470        480 
LHFPPSEALK LWGYPVDESD ITSLFQKHIM SDISAIPWID EPVEVETKTI AKYLLKLNGN 

       490        500        510        520        530        540 
SWWTVGSQPA VNGAPSADPV FGWGPKGGRV FQKAFVECFV NGKDLKDFIT KWHDNPQVTY 

       550        560        570        580        590        600 
YAGNNKSEFL TNAPKDGASA VTWGVYPGRE IIQSTIIAEV SFKAWLSESF QVWGEWANLY 

       610        620        630        640 
SKNTPSRKLL ENCINDRWLV TVIHHDFMDK NGLWKVLEID F 

« 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], 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]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-641.
Strain: PR745.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011686 Genomic DNA. Translation: CAA09738.1.
CU329670 Genomic DNA. Translation: CAB52273.1.
D89118 mRNA. Translation: BAA13780.1.
PIRT38659.
RefSeqNP_593430.1. NM_001018863.2.

3D structure databases

ProteinModelPortalO74927.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279537. 6 interactions.
STRING4896.SPAC343.10-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC343.10.1; SPAC343.10.1:pep; SPAC343.10.
GeneID2543105.
KEGGspo:SPAC343.10.

Organism-specific databases

PomBaseSPAC343.10.

Phylogenomic databases

eggNOGCOG0685.
HOGENOMHOG000246234.
KOK00297.
OMANVTWGAG.
OrthoDBEOG7M0P15.
PhylomeDBO74927.

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

NextBio20804132.

Entry information

Entry nameMTHR2_SCHPO
AccessionPrimary (citable) accession number: O74927
Secondary accession number(s): P78770, Q9UT80
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 14, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 2 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