Reviewed, UniProtKB/Swiss-Prot Q10258 (MTHR1_SCHPO)

Names and origin

Protein names

Recommended name:
    Methylenetetrahydrofolate reductase 1
    EC=1.5.1.20

Gene names

Name:	met9
ORF Names:	SPAC56F8.10

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 pathway.
Sequence similarities	Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Ref.1 Inferred from direct assay. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	methylenetetrahydrofolate reductase (NADPH) activity Inferred from direct assay. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 603	603	Methylenetetrahydrofolate reductase 1		PRO_0000190253
Amino acid modifications
	Modified residue	355	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q10258-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 38519FEE783D331F	FASTA	603	69,012
	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

References

	« Hide 'large scale' referencesShow '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: 12112238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA93581.1.
PIR	T38920.
RefSeq	NP_593224.1.
3D structure databases
HSSP	HSSP built from PDB template 1B5T based on UniProtKB P00394.
ModBase	Search...
Genome annotation databases
GeneID	2542993.
KEGG	spo:SPAC56F8.10.
NMPDR	fig|4896.1.peg.3194.
Organism-specific databases
GeneDB_Spombe	SPAC56F8.10.
Phylogenomic databases
OMA	Q10258. DITWHPA.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000918-MON.
BRENDA	1.5.1.20. 653.
Gene expression databases
ArrayExpress	Q10258.
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...

Entry information

Entry name

MTHR1_SCHPO

Accession

Primary (citable) accession number: Q10258

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)