Reviewed, UniProtKB/Swiss-Prot Q9P786 (MTD1_SCHPO)

Names and origin

Protein names

Recommended name:
    Methylenetetrahydrofolate dehydrogenase [NAD+]
    EC=1.5.1.15

Gene names

Name:	mtd1
ORF Names:	SPBC1711.04

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	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis By similarity.
Catalytic activity	5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH.
Cofactor	NAD By similarity.
Pathway	One-carbon metabolism; tetrahydrofolate pathway.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm. Nucleus. Ref.2
Sequence similarities	Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Ontologies

Keywords
Biological process	One-carbon metabolism Purine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	binding Inferred from electronic annotation. Source: InterPro methylenetetrahydrofolate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 320	320	Methylenetetrahydrofolate dehydrogenase [NAD+]		PRO_0000316023
Regions
	Nucleotide binding	187 – 188	2	NAD By similarity
	Nucleotide binding	210 – 211	2	NAD By similarity
Sites
	Active site	152	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9P786-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 34BBB0B287D8B928	FASTA	320	35,814
	10 20 30 40 50 60 MSNTNKSEPN HSCKVVYASR VAETFVEQLK QHVNLFEFAP KLVGFLSNSD PAARMYADWT 70 80 90 100 110 120 NKTCTEIGFQ YELREVPKDD LEDAIVEANN DPSVNGIMIY FPVFNDGQDQ YLQQVVSPDK 130 140 150 160 170 180 DVEGLCHKYV MNMYHNIRHL DPEKTKKSIL PCTPLAIVKI LEYLGVYNKI INYGNRLYGK 190 200 210 220 230 240 TITIVNRSEI VGRPLAALLA NDGAKVYSVD IHNVQCFTRG AGIRSKKHDV ADTNFKLEDV 250 260 270 280 290 300 APISDVIICG VPSANYKFPS NLVRDGAVCI CFSSEKNFDA ASLKEHAGIY VPSIGKVTIA 310 320 MLLRNLIRLT SYQLNKPVDI

References

[1]

"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.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAB88234.1.
RefSeq	NP_595877.1.
3D structure databases
HSSP	HSSP built from PDB template 1EDZ based on UniProtKB Q02046.
ModBase	Search...
Genome annotation databases
GeneID	2539884.
KEGG	spo:SPBC1711.04.
NMPDR	fig|4896.1.peg.1743.
Organism-specific databases
GeneDB_Spombe	SPBC1711.04.
Phylogenomic databases
OMA	Q9P786. VCINFSS.
Enzyme and pathway databases
BRENDA	1.5.1.15. 653.
Gene expression databases
ArrayExpress	Q9P786.
Family and domain databases
InterPro	IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view]
PRINTS	PR00085. THFDHDRGNASE.
ProDom	PD002300. THFDhg/Cyc_hydro. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

MTD1_SCHPO

Accession

Primary (citable) accession number: Q9P786

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)