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UniProtKB/Swiss-Prot entry P09440


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

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Entry information
Entry name C1TM_YEAST
Primary accession number P09440
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 90)
Name and origin of the protein
Protein name C-1-tetrahydrofolate synthase, mitochondrial [Precursor]
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: MIS1
OrderedLocusNames: YBR084W
ORFNames: YBR0751
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=2836393 [NCBI, ExPASy, EBI, Israel, Japan]
Shannon K.W., Rabinowitz J.C.;
"Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase.";
J. Biol. Chem. 263:7717-7725(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
PROTEIN SEQUENCE OF 35-74, CHARACTERIZATION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=3528153 [NCBI, ExPASy, EBI, Israel, Japan]
Shannon K.W., Rabinowitz J.C.;
"Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae.";
J. Biol. Chem. 261:12266-12271(1986).
[4]
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).
[5]
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).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, 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
Z35953; CAA85029.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03724; AAA34781.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28174; A28174.
RefSeq NP_009640.1; -.
3D structure databases
HSSP P11586; 1A4I. [HSSP ENTRY / PDB]
ModBase P09440.
Protein-protein interaction databases
DIP DIP:6724N; -.
Organism-specific databases
CYGD YBR084w; -.
SGD S000000288; MIS1.
Yeast-GFP YBR084W.
Gene expression databases
ArrayExpress P09440; -.
GermOnline YBR084W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004329; Molecular function: formate-tetrahydrofolate ligase activity (inferred from electronic annotation from InterPro).
GO:0004477; Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from electronic annotation from EC).
GO:0004488; Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0001718; Biological process: conversion of met-tRNAf to fmet-tRNA (inferred from mutant phenotype from SGD).
GO:0046656; Biological process: folic acid biosynthetic process (inferred from direct assay from SGD).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086; Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006164; Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
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.
Proteomic databases
PeptideAtlas P09440; -.
Genome annotation databases
Ensembl YBR084W; Saccharomyces cerevisiae. [Contig view]
GeneID 852378; -.
GenomeReviews Y13134_GR; YBR084W.
KEGG sce:YBR084W; -.
NMPDR fig|4932.3.peg.338; -.
Phylogenomic databases
HOGENOM P09440; -.
Other
LinkHub P09440; -.
NextBio 971174; -.
ProtoNet P09440.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; ATP-binding; Complete proteome; Direct protein sequencing; Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis; Mitochondrion; Multifunctional enzyme; NADP; Nucleotide-binding; One-carbon metabolism; Oxidoreductase; Phosphoprotein; Purine biosynthesis; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    34  34     Mitochondrion. 
CHAIN   35   975  941     C-1-tetrahydrofolate synthase, mitochondrial. PRO_0000034052
NP_BIND   201   203  3     NADP (By similarity). 
NP_BIND   408   415  8     ATP (By similarity). 
REGION   35   343  309     Methylenetetrahydrofolate dehydrogenase and cyclohydrolase. 
REGION   83    87  5     Substrate binding (By similarity). 
REGION   130   132  3     Substrate binding (By similarity). 
REGION   301   305  5     Substrate binding (By similarity). 
REGION   344   975  632     Formyltetrahydrofolate synthetase. 
BINDING   226   226        NADP (By similarity). 
MOD_RES   521   521        Phosphoserine. 
Sequence information
Length: 975 AA [This is the length of the unprocessed precursor] Molecular weight: 106217 Da [This is the MW of the unprocessed precursor] CRC64: B9421D4F8981531F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSRLSLLSN SRAFQQARWR IYRLKVSPTV HASQYHILSG RKLAQSIREK ANDEIQAIKL 

        70         80         90        100        110        120 
KHPNFKPTLK IIQVGARPDS STYVRMKLKA SKDSNVDCII EKLPAEITEV ELLKKISDIN 

       130        140        150        160        170        180 
DDDSIHGLLI QLPLPRHLDE TTITNAVDFK KDVDGFHRYN AGELAKKGGK PYFIPCTPYG 

       190        200        210        220        230        240 
CMKLLEEAHV KLDGKNAVVL GRSSIVGNPI ASLLKNANAT VTVCHSHTRN IAEVVSQADI 

       250        260        270        280        290        300 
VIAACGIPQY VKSDWIKEGA VVIDVGINYV PDISKKSGQK LVGDVDFDSV KEKTSYITPV 

       310        320        330        340        350        360 
PGGVGPMTVA MLVSNVLLAA KRQFVESEKL PVIKPLPLHL ESPVPSDIDI SRAQSPKHIK 

       370        380        390        400        410        420 
QVAEELGIHS HELELYGHYK AKISPNIFKR LESRENGKYV LVAGITPTPL GEGKSTTTMG 

       430        440        450        460        470        480 
LVQALSAHLG KPSIANVRQP SLGPTLGVKG GAAGGGYAQV IPMDEFNLHL TGDIHAISAA 

       490        500        510        520        530        540 
NNLLAAAIDT RMFHEATQKN DSTFYKRLVP RKKGIRKFTP SMQRRLKRLD IEKEDPDALT 

       550        560        570        580        590        600 
PEEVKRFARL NINPDTITIR RVVDINDRML RQITIGEAAT EKGFTRTTGF DITVASELMA 

       610        620        630        640        650        660 
ILALSKSLHE MKERIGRMVI GADYDNKPVT VEDIGCTGAL TALLRDAIKP NLMQTLEGTP 

       670        680        690        700        710        720 
VMVHAGPFAN ISIGASSVIA DLMALKLVGS EKNPLNDKNI HEPGYVVTEA GFDFAMGGER 

       730        740        750        760        770        780 
FFDIKCRSSG LVPDAVVLVA TVRALKSHGG APNVKPGQSL PKEYTEENID FVAKGVSNLV 

       790        800        810        820        830        840 
KQIENIKTFG IPVVVAINRF ETDSQAEIEV IKKAALNAGA SHAVTSNHWM EGGKGAVELA 

       850        860        870        880        890        900 
HAVVDATKEP KNFNFLYDVN SSIEDKLTSI VQKMYGGAKI EVSPEAQKKI DTYKKQGFGN 

       910        920        930        940        950        960 
LPICIAKTQY SLSHDPSLKG VPRGFTFPIR DVRASIGAGY LYALAAEIQT IPGLSTYAGY 

       970 
MAVEVDDDGE IEGLF 

P09440 in FASTA format

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