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UniProtKB/Swiss-Prot entry P07245


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

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Entry information
Entry name C1TC_YEAST
Primary accession number P07245
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on April 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 94)
Name and origin of the protein
Protein name C-1-tetrahydrofolate synthase, cytoplasmic
Synonym C1-THF synthase
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Formyltetrahydrofolate synthetase
     (EC 6.3.4.3)
Gene name
Name: ADE3
OrderedLocusNames: YGR204W
ORFNames: G7733
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].
PubMed=3514599 [NCBI, ExPASy, EBI, Israel, Japan]
Staben C., Rabinowitz J.C.;
"Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase.";
J. Biol. Chem. 261:4629-4637(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<273::AID-YEA898>3.3.CO;2-T; PubMed=8904340 [NCBI, ExPASy, EBI, Israel, Japan]
Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.;
"Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs.";
Yeast 12:273-280(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
MUTAGENESIS.
DOI=10.1021/bi00431a020; PubMed=2541774 [NCBI, ExPASy, EBI, Israel, Japan]
Barlowe C.K., Williams M.E., Rabinowitz J.C., Appling D.R.;
"Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme.";
Biochemistry 28:2099-2106(1989).
[6]
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; THR-318; SER-322; THR-384 AND THR-894, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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
M12878; AAA66316.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49133; CAA88997.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72989; CAA97231.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692966; AAT92985.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29550; A29550.
RefSeq NP_011720.1; -.
3D structure databases
HSSP P11586; 1A4I. [HSSP ENTRY / PDB]
ModBase P07245.
Protein-protein interaction databases
DIP DIP:3867N; -.
IntAct P07245; -.
Organism-specific databases
CYGD YGR204w; -.
SGD S000003436; ADE3.
Yeast-GFP YGR204W.
Gene expression databases
ArrayExpress P07245; -.
GermOnline YGR204W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0004329; Molecular function: formate-tetrahydrofolate ligase activity (inferred from mutant phenotype from SGD).
GO:0004477; Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from mutant phenotype from SGD).
GO:0004488; Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from mutant phenotype from SGD).
GO:0009113; Biological process: purine base biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000559; Fmtethyd_synth.
IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01268; FTHFS; 1.
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]
PROSITE PS00721; FTHFS_1; 1.
PS00722; FTHFS_2; 1.
PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.
BLOCKS P07245.
ProtoNet P07245.
Proteomic databases
PeptideAtlas P07245; -.
Genome annotation databases
Ensembl YGR204W; Saccharomyces cerevisiae. [Contig view]
GeneID 853118; -.
GenomeReviews Y13135_GR; YGR204W.
KEGG sce:YGR204W; -.
NMPDR fig|4932.3.peg.2847; -.
Phylogenomic databases
HOGENOM P07245; -.
Other
LinkHub P07245; -.
NextBio 973148; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding; Nucleus; One-carbon metabolism; Oxidoreductase; Phosphoprotein; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   946  946     C-1-tetrahydrofolate synthase, cytoplasmic. PRO_0000199326
NP_BIND   169   171  3     NADP (By similarity). 
NP_BIND   384   391  8     ATP (By similarity). 
REGION   1   319  319     Methylenetetrahydrofolate dehydrogenase and cyclohydrolase. 
REGION   51    55  5     Substrate binding (By similarity). 
REGION   98   100  3     Substrate binding (By similarity). 
REGION   277   281  5     Substrate binding (By similarity). 
REGION   320   946  627     Formyltetrahydrofolate synthetase. 
BINDING   194   194        NADP (By similarity). 
MOD_RES   176   176        Phosphoserine. 
MOD_RES   318   318        Phosphothreonine. 
MOD_RES   322   322        Phosphoserine. 
MOD_RES   384   384        Phosphothreonine. 
MOD_RES   894   894        Phosphothreonine. 
MUTAGEN   11    11        C->S: Almost no effect on activity. 
MUTAGEN   144   144        C->S: Cyclohydrolase activity is reduced 20-fold. Dehydrogenase Km is increased 7-fold. 
MUTAGEN   257   257        C->S: Cyclohydrolase activity is increased 2-fold. Dehydrogenase Km is increased 2-fold. 
Sequence information
Length: 946 AA [This is the length of the unprocessed precursor] Molecular weight: 102205 Da [This is the MW of the unprocessed precursor] CRC64: BC2897EC380CBA6F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGQVLDGKA CAQQFRSNIA NEIKSIQGHV PGFAPNLAII QVGNRPDSAT YVRMKRKAAE 

        70         80         90        100        110        120 
EAGIVANFIH LDESATEFEV LRYVDQLNED PHTHGIIVQL PLPAHLDEDR ITSRVLAEKD 

       130        140        150        160        170        180 
VDGFGPTNIG ELNKKNGHPF FLPCTPKGII ELLHKANVTI EGSRSVVIGR SDIVGSPVAE 

       190        200        210        220        230        240 
LLKSLNSTVT ITHSKTRDIA SYLHDADIVV VAIGQPEFVK GEWFKPRDGT SSDKKTVVID 

       250        260        270        280        290        300 
VGTNYVADPS KKSGFKCVGD VEFNEAIKYV HLITPVPGGV GPMTVAMLMQ NTLIAAKRQM 

       310        320        330        340        350        360 
EESSKPLQIP PLPLKLLTPV PSDIDISRAQ QPKLINQLAQ ELGIYSHELE LYGHYKAKIS 

       370        380        390        400        410        420 
PKVIERLQTR QNGKYILVSG ITPTPLGEGK STTTMGLVQA LTAHLGKPAI ANVRQPSLGP 

       430        440        450        460        470        480 
TLGVKGGAAG GGYSQVIPMD EFNLHLTGDI HAIGAANNLL AAAIDTRMFH ETTQKNDATF 

       490        500        510        520        530        540 
YNRLVPRKNG KRKFTPSMQR RLNRLGIQKT NPDDLTPEEI NKFARLNIDP DTITIKRVVD 

       550        560        570        580        590        600 
INDRMLRQIT IGQAPTEKNH TRVTGFDITV ASELMAILAL SKDLRDMKER IGRVVVAADV 

       610        620        630        640        650        660 
NRSPVTVEDV GCTGALTALL RDAIKPNLMQ TLEGTPVLVH AGPFANISIG ASSVIADRVA 

       670        680        690        700        710        720 
LKLVGTEPEA KTEAGYVVTE AGFDFTMGGE RFFNIKCRSS GLTPNAVVLV ATVRALKSHG 

       730        740        750        760        770        780 
GAPDVKPGQP LPSAYTEENI EFVEKGAANM CKQIANIKQF GVPVVVAINK FETDTEGEIA 

       790        800        810        820        830        840 
AIRKAALEAG AFEAVTSNHW AEGGKGAIDL AKAVIEASNQ PVDFHFLYDV NSSVEDKLTT 

       850        860        870        880        890        900 
IVQKMYGGAA IDILPEAQRK IDMYKEQGFG NLPICIAKTQ YSLSHDATLK GVPTGFTFPI 

       910        920        930        940 
RDVRLSNGAG YLYALAAEIQ TIPGLATYAG YMAVEVDDDG EIDGLF 

P07245 in FASTA format

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