MTD1_SCHPO
ID MTD1_SCHPO Reviewed; 320 AA.
AC Q9P786;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase [NAD(+)];
DE EC=1.5.1.15;
GN Name=mtd1; ORFNames=SPBC1711.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes oxidation of cytoplasmic one-carbon units for
CC purine biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-
CC methenyltetrahydrofolate + NADH; Xref=Rhea:RHEA:22892,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.5.1.15;
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB88234.1; -; Genomic_DNA.
DR RefSeq; NP_595877.1; NM_001021783.2.
DR AlphaFoldDB; Q9P786; -.
DR SMR; Q9P786; -.
DR BioGRID; 276430; 4.
DR STRING; 4896.SPBC1711.04.1; -.
DR iPTMnet; Q9P786; -.
DR MaxQB; Q9P786; -.
DR PaxDb; Q9P786; -.
DR PRIDE; Q9P786; -.
DR EnsemblFungi; SPBC1711.04.1; SPBC1711.04.1:pep; SPBC1711.04.
DR GeneID; 2539884; -.
DR KEGG; spo:SPBC1711.04; -.
DR PomBase; SPBC1711.04; mtd1.
DR VEuPathDB; FungiDB:SPBC1711.04; -.
DR eggNOG; KOG0089; Eukaryota.
DR HOGENOM; CLU_031413_0_0_1; -.
DR InParanoid; Q9P786; -.
DR OMA; CKVITAE; -.
DR PhylomeDB; Q9P786; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:Q9P786; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; ISO:PomBase.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0046656; P:folic acid biosynthetic process; ISO:PomBase.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; ISO:PomBase.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd01079; NAD_bind_m-THF_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR035812; m-THF_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Nucleus; One-carbon metabolism; Oxidoreductase;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..320
FT /note="Methylenetetrahydrofolate dehydrogenase [NAD(+)]"
FT /id="PRO_0000316023"
FT ACT_SITE 152
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 35814 MW; 34BBB0B287D8B928 CRC64;
MSNTNKSEPN HSCKVVYASR VAETFVEQLK QHVNLFEFAP KLVGFLSNSD PAARMYADWT
NKTCTEIGFQ YELREVPKDD LEDAIVEANN DPSVNGIMIY FPVFNDGQDQ YLQQVVSPDK
DVEGLCHKYV MNMYHNIRHL DPEKTKKSIL PCTPLAIVKI LEYLGVYNKI INYGNRLYGK
TITIVNRSEI VGRPLAALLA NDGAKVYSVD IHNVQCFTRG AGIRSKKHDV ADTNFKLEDV
APISDVIICG VPSANYKFPS NLVRDGAVCI CFSSEKNFDA ASLKEHAGIY VPSIGKVTIA
MLLRNLIRLT SYQLNKPVDI
