AIM17_YEAST
ID AIM17_YEAST Reviewed; 465 AA.
AC P23180; D3DKP4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable oxidoreductase AIM17;
DE EC=1.14.11.-;
DE AltName: Full=Altered inheritance of mitochondria protein 17, mitochondrial;
DE AltName: Full=Found in mitochondrial proteome protein 12;
DE Flags: Precursor;
GN Name=AIM17; Synonyms=FMP12; OrderedLocusNames=YHL021C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-465.
RX PubMed=3317399; DOI=10.1073/pnas.84.22.8035;
RA Atcheson C.L., Didomenico B., Frackman S., Esposito R.E., Elder R.T.;
RT "Isolation, DNA sequence, and regulation of a meiosis-specific eukaryotic
RT recombination gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8035-8039(1987).
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 DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [7]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND DEGRADATION.
RX PubMed=20150421; DOI=10.1074/jbc.m109.065425;
RA Bayot A., Gareil M., Rogowska-Wrzesinska A., Roepstorff P., Friguet B.,
RA Bulteau A.L.;
RT "Identification of novel oxidized protein substrates and physiological
RT partners of the mitochondrial ATP-dependent Lon-like protease Pim1.";
RL J. Biol. Chem. 285:11445-11457(2010).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:20150421}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- MISCELLANEOUS: Present with 5800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Accumulates as a carbonylated protein in absence of
CC PIM1, suggesting that the PIM1 protease is responsible for the
CC degradation of its oxidized form in mitochondria.
CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR EMBL; U11582; AAB65074.1; -; Genomic_DNA.
DR EMBL; J02987; AAA65531.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06664.1; -; Genomic_DNA.
DR PIR; S46835; S46835.
DR RefSeq; NP_011842.1; NM_001179101.1.
DR AlphaFoldDB; P23180; -.
DR SMR; P23180; -.
DR BioGRID; 36402; 122.
DR DIP; DIP-4919N; -.
DR IntAct; P23180; 4.
DR STRING; 4932.YHL021C; -.
DR MaxQB; P23180; -.
DR PaxDb; P23180; -.
DR PRIDE; P23180; -.
DR EnsemblFungi; YHL021C_mRNA; YHL021C; YHL021C.
DR GeneID; 856365; -.
DR KEGG; sce:YHL021C; -.
DR SGD; S000001013; AIM17.
DR VEuPathDB; FungiDB:YHL021C; -.
DR eggNOG; KOG3888; Eukaryota.
DR GeneTree; ENSGT00530000063582; -.
DR HOGENOM; CLU_021859_0_1_1; -.
DR InParanoid; P23180; -.
DR OMA; SVNILHC; -.
DR BioCyc; YEAST:G3O-31041-MON; -.
DR Reactome; R-SCE-71262; Carnitine synthesis.
DR PRO; PR:P23180; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P23180; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045329; P:carnitine biosynthetic process; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..465
FT /note="Probable oxidoreductase AIM17"
FT /id="PRO_0000207092"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 53135 MW; 568B17051DB60899 CRC64;
MLRSNLCRGS RILARLTTTP RTYTSAATAA AANRGHIIKT YFNRDSTTIT FSMEESSKPV
SVCFNNVFLR DASHSAKLVT TGELYHNEKL TAPQDIQISE DGKSLVVKWK DGGHHQFPLQ
FFIDYKGSSF VSPATRKQES RYRPQLWNKR ILKDNVKDLL SVSYNEFIDP KDDSKLFQTL
VNLQKFGIAF ISGTPSSSSE GLTIQKICER IGPIRSTVHG EGTFDVNASQ ATSVNAHYAN
KDLPLHTDLP FLENVPGFQI LQSLPATEGE DPNTRPMNYF VDAFYATRNV RESDFEAYEA
LQIVPVNYIY ENGDKRYYQS KPLIEHHDIN EDNTLLGNYE ALIKCINYSP PYQAPFTFGI
YDKPSDLNNN LDLNLITTPA KLTERFLFKS FIRGLNLFES HINDFNNQFR LQLPENCCVI
FNNRRILHAN SLTSSNQQWL KGCYFDSDTF KSKLKFLEEK FPHDK
