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UniProtKB/Swiss-Prot entry Q02046


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTD1_YEAST
Primary accession number Q02046
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 74)
Name and origin of the protein
Protein name Methylenetetrahydrofolate dehydrogenase [NAD+]
Synonym EC 1.5.1.15
Gene name
Name: MTD1
OrderedLocusNames: YKR080W
ORFNames: YKR400
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 72-86 AND 146-160.
PubMed=8416923 [NCBI, ExPASy, EBI, Israel, Japan]
West M.G., Barlowe C.K., Appling D.R.;
"Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase.";
J. Biol. Chem. 268:153-160(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
PubMed=8203164 [NCBI, ExPASy, EBI, Israel, Japan]
Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G., Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
"The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open reading frames.";
Yeast 10:231-245(1994).
[4]
IDENTIFICATION OF PROTEIN.
DOI=10.1021/bi00482a020; PubMed=2223762 [NCBI, ExPASy, EBI, Israel, Japan]
Barlowe C.K., Appling D.R.;
"Isolation and characterization of a novel eukaryotic monofunctional NAD(+)-dependent 5,10-methylenetetrahydrofolate dehydrogenase.";
Biochemistry 29:7089-7094(1990).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
PubMed=10933503 [NCBI, ExPASy, EBI, Israel, Japan]
Monzingo A.F., Breksa A., Ernst S., Appling D.R., Robertus J.D.;
"The X-ray structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae.";
Protein Sci. 9:1374-1381(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L02934; AAB00323.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z27116; CAA81631.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z28305; CAA82159.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S31254; S31254.
RefSeq NP_013006.1; -.
3D structure databases
PDB
1EDZ; X-ray; 2.80 A; A=1-320.[ExPASy / RCSB / EBI]
1EE9; X-ray; 3.00 A; A=1-320.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EDZ; -.
1EE9; -.
ModBase Q02046.
Protein-protein interaction databases
DIP DIP:730N; -.
Organism-specific databases
CYGD YKR080w; -.
SGD S000001788; MTD1.
Yeast-GFP YKR080W.
Gene expression databases
ArrayExpress Q02046; -.
GermOnline YKR080W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0004487; Molecular function: methylenetetrahydrofolate dehydrogenase (NAD+) activity (inferred from mutant phenotype from SGD).
GO:0009396; Biological process: folic acid and derivative biosynthetic process (inferred from mutant phenotype from SGD).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from direct assay from SGD).
GO:0009113; Biological process: purine base biosynthetic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q02046.
Proteomic databases
PeptideAtlas Q02046; -.
Genome annotation databases
Ensembl YKR080W; Saccharomyces cerevisiae. [Contig view]
GeneID 853955; -.
GenomeReviews Y13137_GR; YKR080W.
KEGG sce:YKR080W; -.
NMPDR fig|4932.3.peg.3993; -.
Phylogenomic databases
HOGENOM Q02046; -.
Other
LinkHub Q02046; -.
ProtoNet Q02046.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; NAD; Nucleus; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   320  320     Methylenetetrahydrofolate dehydrogenase [NAD+]. PRO_0000199319
NP_BIND   185   186  2     NAD. 
NP_BIND   208   209  2     NAD. 
NP_BIND   274   276  3     NAD. 
ACT_SITE   150   150        By similarity. 
HELIX   10    31  22      
TURN   32    34  3      
STRAND   38    43  6      
HELIX   48    63  16      
STRAND   67    72  6      
HELIX   76    78  3      
HELIX   79    88  10      
STRAND   94    97  4      
STRAND   101   104  4      
HELIX   105   110  6      
TURN   111   113  3      
TURN   116   118  3      
HELIX   125   132  8      
STRAND   137   142  6      
HELIX   150   161  12      
TURN   174   177  4      
STRAND   179   183  5      
TURN   187   189  3      
HELIX   190   198  9      
STRAND   203   207  5      
STRAND   209   217  9      
STRAND   227   233  7      
HELIX   236   245  10      
STRAND   247   251  5      
TURN   262   264  3      
STRAND   269   273  5      
STRAND   275   277  3      
HELIX   282   285  4      
STRAND   288   293  6      
HELIX   296   316  21      
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 36240 Da [This is the MW of the unprocessed precursor] CRC64: DA30D9E2CEB590C6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKPGRTILA SKVAETFNTE IINNVEEYKK THNGQGPLLV GFLANNDPAA KMYATWTQKT 

        70         80         90        100        110        120 
SESMGFRYDL RVIEDKDFLE EAIIQANGDD SVNGIMVYFP VFGNAQDQYL QQVVCKEKDV 

       130        140        150        160        170        180 
EGLNHVYYQN LYHNVRYLDK ENRLKSILPC TPLAIVKILE FLKIYNNLLP EGNRLYGKKC 

       190        200        210        220        230        240 
IVINRSEIVG RPLAALLAND GATVYSVDVN NIQKFTRGES LKLNKHHVED LGEYSEDLLK 

       250        260        270        280        290        300 
KCSLDSDVVI TGVPSENYKF PTEYIKEGAV CINFACTKNF SDDVKEKASL YVPMTGKVTI 

       310        320 
AMLLRNMLRL VRNVELSKEK 

Q02046 in FASTA format

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