TMT1_YEAST
ID TMT1_YEAST Reviewed; 299 AA.
AC P32643; D3DM83;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Trans-aconitate 3-methyltransferase;
DE EC=2.1.1.145 {ECO:0000269|PubMed:11695919};
GN Name=TMT1; Synonyms=TAM1; OrderedLocusNames=YER175C; ORFNames=SYGP-ORF63;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11695919; DOI=10.1021/bi011380j;
RA Cai H., Dumlao D.S., Katz J.E., Clarke S.;
RT "Identification of the gene and characterization of the activity of the
RT trans-aconitate methyltransferase from Saccharomyces cerevisiae.";
RL Biochemistry 40:13699-13709(2001).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15147181; DOI=10.1021/bi049784+;
RA Katz J.E., Dumlao D.S., Wasserman J.I., Lansdown M.G., Jung M.E.,
RA Faull K.F., Clarke S.;
RT "3-isopropylmalate is the major endogenous substrate of the Saccharomyces
RT cerevisiae trans-aconitate methyltransferase.";
RL Biochemistry 43:5976-5986(2004).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=18092814; DOI=10.1021/bi7018157;
RA Dumlao D.S., Hertz N., Clarke S.;
RT "Secreted 3-isopropylmalate methyl ester signals invasive growth during
RT amino acid starvation in Saccharomyces cerevisiae.";
RL Biochemistry 47:698-709(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC of trans-aconitate and 3-isopropylmalate at high affinity and of other
CC molecules like cis-aconitate, isocitrate, and citrate at lower
CC velocities and affinities. The function of trans-aconitate methylation
CC appears to be in reducing the toxicity of this spontaneous breakdown
CC product of cis-aconitate. The role of 3-isopropylmalate methylation is
CC unclear but may represent a metabolic branch at 3-isopropylmalate,
CC where some of the material is taken in the pathway leading to leucine
CC and some is taken in a pathway to the 3-isopropylmalate methyl ester, a
CC molecule that provides a signal to switch from vegetative to invasive
CC growth in response to amino acid starvation.
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181,
CC ECO:0000269|PubMed:18092814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-aconitate = (E)-2-
CC (methoxycarbonylmethyl)but-2-enedioate + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:22200, ChEBI:CHEBI:15708, ChEBI:CHEBI:57469,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.145;
CC Evidence={ECO:0000269|PubMed:11695919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22201;
CC Evidence={ECO:0000305|PubMed:11695919};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=660 uM for trans-aconitate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=74000 uM for cis-aconitate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=44000 uM for itaconate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=323 uM for isopropylmaleate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=1670 uM for isopropylfumarate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=127 uM for (2R,3S)-3-isopropylmalate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=341 uM for (2S,3R)-3-isopropylmalate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC KM=428 uM for (2R,3R)/(2S,3S)-3-isopropylmalate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC KM=19 uM for 2-(1-methylethylidine)succinate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC KM=45 uM for 3-butylmalate {ECO:0000269|PubMed:11695919,
CC ECO:0000269|PubMed:15147181};
CC Vmax=44.8 nmol/min/mg enzyme with trans-aconitate as substrate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=12.1 nmol/min/mg enzyme with cis-aconitate as substrate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=26.9 nmol/min/mg enzyme with itaconate as substrate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=39.7 nmol/min/mg enzyme with isopropylmaleate as substrate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=2.4 nmol/min/mg enzyme with isopropylfumarate as substrate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=59.2 nmol/min/mg enzyme with (2R,3S)-3-isopropylmalate as
CC substrate {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=77.8 nmol/min/mg enzyme with (2S,3R)-3-isopropylmalate as
CC substrate {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=4.4 nmol/min/mg enzyme with (2R,3R)/(2S,3S)-3-isopropylmalate as
CC substrate {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=36.2 nmol/min/mg enzyme with 2-(1-methylethylidine)succinate as
CC substrate {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC Vmax=40.4 nmol/min/mg enzyme with 3-butylmalate as substrate
CC {ECO:0000269|PubMed:11695919, ECO:0000269|PubMed:15147181};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: During amino acid starvation. {ECO:0000269|PubMed:18092814}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC {ECO:0000305}.
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DR EMBL; U18922; AAB64702.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07837.1; -; Genomic_DNA.
DR PIR; S30861; S30861.
DR RefSeq; NP_011102.3; NM_001179065.3.
DR PDB; 3G5T; X-ray; 1.12 A; A=2-299.
DR PDBsum; 3G5T; -.
DR AlphaFoldDB; P32643; -.
DR SMR; P32643; -.
DR BioGRID; 36928; 53.
DR DIP; DIP-4807N; -.
DR STRING; 4932.YER175C; -.
DR iPTMnet; P32643; -.
DR MaxQB; P32643; -.
DR PaxDb; P32643; -.
DR PRIDE; P32643; -.
DR EnsemblFungi; YER175C_mRNA; YER175C; YER175C.
DR GeneID; 856922; -.
DR KEGG; sce:YER175C; -.
DR SGD; S000000977; TMT1.
DR VEuPathDB; FungiDB:YER175C; -.
DR eggNOG; KOG3010; Eukaryota.
DR GeneTree; ENSGT00940000176672; -.
DR HOGENOM; CLU_049344_1_2_1; -.
DR InParanoid; P32643; -.
DR OMA; RTWSAYH; -.
DR BioCyc; MetaCyc:YER175C-MON; -.
DR BioCyc; YEAST:YER175C-MON; -.
DR SABIO-RK; P32643; -.
DR EvolutionaryTrace; P32643; -.
DR PRO; PR:P32643; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32643; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0046547; F:trans-aconitate 3-methyltransferase activity; IDA:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..299
FT /note="Trans-aconitate 3-methyltransferase"
FT /id="PRO_0000202658"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3G5T"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3G5T"
FT TURN 85..90
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3G5T"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 139..154
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:3G5T"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3G5T"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:3G5T"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3G5T"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:3G5T"
FT STRAND 285..298
FT /evidence="ECO:0007829|PDB:3G5T"
SQ SEQUENCE 299 AA; 34768 MW; 50647D67F9A61629 CRC64;
MSTFSASDFN SERYSSSRPS YPSDFYKMID EYHDGERKLL VDVGCGPGTA TLQMAQELKP
FEQIIGSDLS ATMIKTAEVI KEGSPDTYKN VSFKISSSDD FKFLGADSVD KQKIDMITAV
ECAHWFDFEK FQRSAYANLR KDGTIAIWGY ADPIFPDYPE FDDLMIEVPY GKQGLGPYWE
QPGRSRLRNM LKDSHLDPEL FHDIQVSYFC AEDVRDKVKL HQHTKKPLLI RKQVTLVEFA
DYVRTWSAYH QWKQDPKNKD KEDVADWFIK ESLRRRPELS TNTKIEVVWN TFYKLGKRV
