FMT_YEAST
ID FMT_YEAST Reviewed; 401 AA.
AC P32785; D6VPY7; Q6RUA6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Methionyl-tRNA formyltransferase, mitochondrial {ECO:0000303|PubMed:10781559};
DE Short=MtFMT {ECO:0000303|PubMed:10781559};
DE EC=2.1.2.9 {ECO:0000269|PubMed:12549912};
DE Flags: Precursor;
GN Name=FMT1; OrderedLocusNames=YBL013W; ORFNames=YBL0311, YBL0313;
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].
RC STRAIN=ATCC 24657 / D273-10B, and ATCC 90840 / EAY235 / FY23;
RA Williams E.H., Butler C.A., Fox T.D.;
RT "Yeast mitochondrial translation initiation.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1332308; DOI=10.1002/yea.320080911;
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RT "The sequence of an 8 kb segment on the left arm of chromosome II from
RT Saccharomyces cerevisiae identifies five new open reading frames of unknown
RT functions, two tRNA genes and two transposable elements.";
RL Yeast 8:777-785(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=10781559; DOI=10.1128/jb.182.10.2886-2892.2000;
RA Li Y., Holmes W.B., Appling D.R., RajBhandary U.L.;
RT "Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria
RT without formylation of the initiator tRNA.";
RL J. Bacteriol. 182:2886-2892(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=W303;
RX PubMed=12549912; DOI=10.1021/bi026901x;
RA Vial L., Gomez P., Panvert M., Schmitt E., Blanquet S., Mechulam Y.;
RT "Mitochondrial methionyl-tRNAfMet formyltransferase from Saccharomyces
RT cerevisiae: gene disruption and tRNA substrate specificity.";
RL Biochemistry 42:932-939(2003).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=30409808; DOI=10.1126/science.aat0174;
RA Kim J.M., Seok O.H., Ju S., Heo J.E., Yeom J., Kim D.S., Yoo J.Y.,
RA Varshavsky A., Lee C., Hwang C.S.;
RT "Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway.";
RL Science 362:0-0(2018).
CC -!- FUNCTION: Formylates methionyl-tRNA in mitochondria and the cytoplasm
CC (PubMed:10781559, PubMed:30409808). Responsible for the formylation of
CC the 8 N-terminally formylated (Nt-formylated) mitochondrial matrix
CC proteins that are encoded by mitochondrial DNA (PubMed:10781559,
CC PubMed:12549912). Nt-formylated proteins in the cytoplasm are strongly
CC up-regulated in stationary phase or upon starvation for specific amino
CC acids (His or Lys) and are targeted for degradation by a PSH1 E3
CC ubiquitin ligase-mediated fMet/N-end rule pathway. Increased Nt-
CC formylation of cytosolic proteins appears to be important for
CC adaptation to these stresses. Stationary phase-degraded Nt-formylated
CC proteins include histone H3-like centromeric protein CSE4, Mediator
CC complex subunit 3 (PGD1) and small ribosomal subunit protein uS8-A
CC (RPS22A) (PubMed:30409808). {ECO:0000269|PubMed:10781559,
CC ECO:0000269|PubMed:12549912, ECO:0000269|PubMed:30409808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC Evidence={ECO:0000269|PubMed:12549912};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for L-methionyl-tRNA(fMet) {ECO:0000269|PubMed:12549912};
CC Note=kcat is 0.13 sec(-1) with L-methionyl-tRNA(fMet) as substrate.
CC {ECO:0000269|PubMed:12549912};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:30409808}.
CC Mitochondrion matrix {ECO:0000269|PubMed:30409808}. Cytoplasm
CC {ECO:0000269|PubMed:30409808}. Note=In exponentially growing cells,
CC more than 97% of FMT1 is present in mitochondria. In stationary phase,
CC about 35% of FMT1 becomes localized to the cytosol in a GCN2-dependent
CC manner. {ECO:0000269|PubMed:30409808}.
CC -!- PTM: Phosphorylated by GCN2 in response to nutrient deprivation.
CC Phosphorylation mediates retention of FMT1 in the cytoplasm.
CC {ECO:0000269|PubMed:30409808}.
CC -!- MISCELLANEOUS: Formylation of the initiator Met-tRNA is not essential
CC for mitochondrial protein synthesis in S.cerevisiae.
CC {ECO:0000269|PubMed:10781559, ECO:0000269|PubMed:12549912}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA84832.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY490279; AAR86694.1; -; Genomic_DNA.
DR EMBL; AY492339; AAR86695.1; -; Genomic_DNA.
DR EMBL; Z35774; CAA84832.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006936; DAA07107.1; -; Genomic_DNA.
DR PIR; S25331; S25331.
DR RefSeq; NP_009540.2; NM_001178253.1.
DR AlphaFoldDB; P32785; -.
DR SMR; P32785; -.
DR BioGRID; 32687; 176.
DR DIP; DIP-8221N; -.
DR IntAct; P32785; 3.
DR STRING; 4932.YBL013W; -.
DR PaxDb; P32785; -.
DR PRIDE; P32785; -.
DR EnsemblFungi; YBL013W_mRNA; YBL013W; YBL013W.
DR GeneID; 852270; -.
DR KEGG; sce:YBL013W; -.
DR SGD; S000000109; FMT1.
DR VEuPathDB; FungiDB:YBL013W; -.
DR eggNOG; KOG3082; Eukaryota.
DR GeneTree; ENSGT00390000017828; -.
DR HOGENOM; CLU_033347_0_1_1; -.
DR OMA; FMPELHA; -.
DR BioCyc; YEAST:G3O-28918-MON; -.
DR BRENDA; 2.1.2.9; 984.
DR PRO; PR:P32785; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32785; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IDA:SGD.
DR GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IDA:SGD.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Mitochondrion; Protein biosynthesis; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..401
FT /note="Methionyl-tRNA formyltransferase, mitochondrial"
FT /id="PRO_0000010096"
FT BINDING 18..20
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P77398"
FT BINDING 66..70
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P77398"
SQ SEQUENCE 401 AA; 44617 MW; 95E1C61C4E6D3AE1 CRC64;
MVKMRRITPT RLLFTCRYIS NNASPPVQPL NVLFFGSDTF SNFSLQALNE LRQNNGSCGI
VDNIQVVTRS PKWCGRQKSI LKYPPIFDMA EKLQLPRPIT CDTKQEMLAL SKLTPSRQGN
PENDGSGAPF NAIIAVSFGK LIPGDLIRAV PLALNVHPSL LPRHKGSAPI QRALLEGDTY
TGVTIQTLHP DRFDHGAIVA QTEPLAIATM LSKGRVNDST ADFNSEGLPR RTAILMDQLG
ALGAQLLGQT LRERLYLPQN RVQAPTAYKP SYAHRITTED KRIHWARDSA AELLNKLETL
GPLHAFKEAT AARKDAQNSV LKRILFHECK VMRDARLDNG SKPGMFKYDD IKDCILVTCR
GNLLLCVSRL QFEGFAVERA GQFMARLRKR CGALSEKLVF L
