MTD1_YEAST
ID MTD1_YEAST Reviewed; 320 AA.
AC Q02046; D6VXE0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase [NAD(+)];
DE EC=1.5.1.15 {ECO:0000269|PubMed:8416923};
GN Name=MTD1; OrderedLocusNames=YKR080W; ORFNames=YKR400;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 72-86 AND 146-160,
RP AND CATALYTIC ACTIVITY.
RX PubMed=8416923; DOI=10.1016/s0021-9258(18)54127-2;
RA West M.G., Barlowe C.K., Appling D.R.;
RT "Cloning and characterization of the Saccharomyces cerevisiae gene encoding
RT NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase.";
RL J. Biol. Chem. 268:153-160(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
RX PubMed=8203164; DOI=10.1002/yea.320100210;
RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G.,
RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae
RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open
RT reading frames.";
RL Yeast 10:231-245(1994).
RN [5]
RP IDENTIFICATION OF PROTEIN.
RX PubMed=2223762; DOI=10.1021/bi00482a020;
RA Barlowe C.K., Appling D.R.;
RT "Isolation and characterization of a novel eukaryotic monofunctional
RT NAD(+)-dependent 5,10-methylenetetrahydrofolate dehydrogenase.";
RL Biochemistry 29:7089-7094(1990).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RX PubMed=10933503; DOI=10.1110/ps.9.7.1374;
RA Monzingo A.F., Breksa A., Ernst S., Appling D.R., Robertus J.D.;
RT "The X-ray structure of the NAD-dependent 5,10-methylenetetrahydrofolate
RT dehydrogenase from Saccharomyces cerevisiae.";
RL Protein Sci. 9:1374-1381(2000).
CC -!- FUNCTION: Catalyzes oxidation of cytoplasmic one-carbon units for
CC purine biosynthesis.
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 Evidence={ECO:0000269|PubMed:8416923};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22893;
CC Evidence={ECO:0000305|PubMed:8416923};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10933503}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 16200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
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DR EMBL; L02934; AAB00323.1; -; Genomic_DNA.
DR EMBL; Z27116; CAA81631.1; -; Genomic_DNA.
DR EMBL; Z28305; CAA82159.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09230.1; -; Genomic_DNA.
DR PIR; S31254; S31254.
DR RefSeq; NP_013006.3; NM_001179870.3.
DR PDB; 1EDZ; X-ray; 2.80 A; A=1-320.
DR PDB; 1EE9; X-ray; 3.00 A; A=1-320.
DR PDBsum; 1EDZ; -.
DR PDBsum; 1EE9; -.
DR AlphaFoldDB; Q02046; -.
DR SMR; Q02046; -.
DR BioGRID; 34211; 39.
DR DIP; DIP-730N; -.
DR IntAct; Q02046; 4.
DR MINT; Q02046; -.
DR STRING; 4932.YKR080W; -.
DR MaxQB; Q02046; -.
DR PaxDb; Q02046; -.
DR PRIDE; Q02046; -.
DR EnsemblFungi; YKR080W_mRNA; YKR080W; YKR080W.
DR GeneID; 853955; -.
DR KEGG; sce:YKR080W; -.
DR SGD; S000001788; MTD1.
DR VEuPathDB; FungiDB:YKR080W; -.
DR eggNOG; KOG0089; Eukaryota.
DR HOGENOM; CLU_031413_0_0_1; -.
DR InParanoid; Q02046; -.
DR OMA; CKVITAE; -.
DR BioCyc; YEAST:YKR080W-MON; -.
DR SABIO-RK; Q02046; -.
DR EvolutionaryTrace; Q02046; -.
DR PRO; PR:Q02046; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02046; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IMP:SGD.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IMP:SGD.
DR GO; GO:0006730; P:one-carbon metabolic process; IDA:SGD.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IDA:SGD.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; NAD; Nucleus;
KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..320
FT /note="Methylenetetrahydrofolate dehydrogenase [NAD(+)]"
FT /id="PRO_0000199319"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10933503"
FT BINDING 208..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10933503"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10933503"
FT HELIX 10..31
FT /evidence="ECO:0007829|PDB:1EDZ"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:1EDZ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1EDZ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1EE9"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:1EDZ"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1EDZ"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1EDZ"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1EDZ"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1EDZ"
FT HELIX 296..316
FT /evidence="ECO:0007829|PDB:1EDZ"
SQ SEQUENCE 320 AA; 36240 MW; DA30D9E2CEB590C6 CRC64;
MSKPGRTILA SKVAETFNTE IINNVEEYKK THNGQGPLLV GFLANNDPAA KMYATWTQKT
SESMGFRYDL RVIEDKDFLE EAIIQANGDD SVNGIMVYFP VFGNAQDQYL QQVVCKEKDV
EGLNHVYYQN LYHNVRYLDK ENRLKSILPC TPLAIVKILE FLKIYNNLLP EGNRLYGKKC
IVINRSEIVG RPLAALLAND GATVYSVDVN NIQKFTRGES LKLNKHHVED LGEYSEDLLK
KCSLDSDVVI TGVPSENYKF PTEYIKEGAV CINFACTKNF SDDVKEKASL YVPMTGKVTI
AMLLRNMLRL VRNVELSKEK
