FMP41_YEAST
ID FMP41_YEAST Reviewed; 259 AA.
AC P53889; D6W114;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Uncharacterized mitochondrial hydrolase FMP41;
DE EC=3.-.-.-;
GN Name=FMP41; OrderedLocusNames=YNL168C; ORFNames=N1696;
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 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [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 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 [7]
RP INDUCTION.
RX PubMed=18495938; DOI=10.1261/rna.864908;
RA Melamed D., Pnueli L., Arava Y.;
RT "Yeast translational response to high salinity: global analysis reveals
RT regulation at multiple levels.";
RL RNA 14:1337-1351(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of yeast hypothetical protein ynq8_yeast.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- INDUCTION: In high salinity conditions. {ECO:0000269|PubMed:18495938}.
CC -!- MISCELLANEOUS: Present with 2550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; X92517; CAA63271.1; -; Genomic_DNA.
DR EMBL; Z71444; CAA96055.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10380.1; -; Genomic_DNA.
DR PIR; S60959; S60959.
DR RefSeq; NP_014231.1; NM_001183006.1.
DR PDB; 1NKQ; X-ray; 2.20 A; A/B/C/D/E/F=1-259.
DR PDBsum; 1NKQ; -.
DR AlphaFoldDB; P53889; -.
DR SMR; P53889; -.
DR BioGRID; 35660; 34.
DR IntAct; P53889; 10.
DR MINT; P53889; -.
DR STRING; 4932.YNL168C; -.
DR MaxQB; P53889; -.
DR PaxDb; P53889; -.
DR PRIDE; P53889; -.
DR EnsemblFungi; YNL168C_mRNA; YNL168C; YNL168C.
DR GeneID; 855553; -.
DR KEGG; sce:YNL168C; -.
DR SGD; S000005112; FMP41.
DR VEuPathDB; FungiDB:YNL168C; -.
DR eggNOG; KOG1535; Eukaryota.
DR GeneTree; ENSGT00940000160452; -.
DR HOGENOM; CLU_028458_5_0_1; -.
DR InParanoid; P53889; -.
DR OMA; YALSIDM; -.
DR BioCyc; YEAST:G3O-33184-MON; -.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR EvolutionaryTrace; P53889; -.
DR PRO; PR:P53889; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53889; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0018773; F:acetylpyruvate hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Mitochondrion; Reference proteome;
KW Stress response.
FT CHAIN 1..259
FT /note="Uncharacterized mitochondrial hydrolase FMP41"
FT /id="PRO_0000156843"
FT BINDING 87
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:1NKQ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1NKQ"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1NKQ"
FT STRAND 238..249
FT /evidence="ECO:0007829|PDB:1NKQ"
SQ SEQUENCE 259 AA; 28792 MW; 6984B5BAB297CECC CRC64;
MSYNYLKAAR KIICIGRNYA AHIKELNNST PKQPFFFLKP TSSIVTPLSS SLVKTTRPAN
STFNGLNEDG TNPGPIFIPR GVKVHHEIEL ALIVSKHLSN VTKMKPEEVY DSISGVALAL
DLTARNVQDE AKKKGLPWTI SKGFDTFMPI SAIVSREKFS SYKSNLQDIF RVKCSVNGQL
RQDGGTNLML HPLHKILQHI STMISLEPGD IILTGTPAGV GELKPGDRVH CELLQNNDNI
VDMNFECENR PGPYEFRET
