ATM1_YEAST
ID ATM1_YEAST Reviewed; 690 AA.
AC P40416; D6W0C8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000305};
DE EC=7.-.-.- {ECO:0000269|PubMed:25006243};
DE Flags: Precursor;
GN Name=ATM1 {ECO:0000312|SGD:S000004916}; Synonyms=MDY {ECO:0000305};
GN OrderedLocusNames=YMR301C; ORFNames=YM9952.03C;
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], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=JK9-3D alpha;
RX PubMed=7828591; DOI=10.1002/j.1460-2075.1995.tb06989.x;
RA Leighton J., Schatz G.;
RT "An ABC transporter in the mitochondrial inner membrane is required for
RT normal growth of yeast.";
RL EMBO J. 14:188-195(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9428742; DOI=10.1016/s0014-5793(97)01414-2;
RA Kispal G., Csere P., Guiard B., Lill R.;
RT "The ABC transporter Atm1p is required for mitochondrial iron
RT homeostasis.";
RL FEBS Lett. 418:346-350(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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=10406803; DOI=10.1093/emboj/18.14.3981;
RA Kispal G., Csere P., Prohl C., Lill R.;
RT "The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of
RT cytosolic Fe/S proteins.";
RL EMBO J. 18:3981-3989(1999).
RN [6]
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 [7]
RP HOMODIMERIZATION, AND MUTAGENESIS OF LYS-475 AND GLU-598.
RX PubMed=15225610; DOI=10.1016/j.febslet.2004.05.051;
RA Chloupkova M., Reaves S.K., LeBard L.M., Koeller D.M.;
RT "The mitochondrial ABC transporter Atm1p functions as a homodimer.";
RL FEBS Lett. 569:65-69(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND MUTAGENESIS OF ARG-216 AND LYS-475.
RX PubMed=25006243; DOI=10.1074/jbc.m114.553438;
RA Schaedler T.A., Thornton J.D., Kruse I., Schwarzlaender M., Meyer A.J.,
RA van Veen H.W., Balk J.;
RT "A conserved mitochondrial ATP-binding cassette transporter exports
RT glutathione polysulfide for cytosolic metal cofactor assembly.";
RL J. Biol. Chem. 289:23264-23274(2014).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31040179; DOI=10.1074/jbc.ra119.008600;
RA Pandey A.K., Pain J., Dancis A., Pain D.;
RT "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm
RT for iron-sulfur cluster assembly and tRNA thiolation in yeast.";
RL J. Biol. Chem. 294:9489-9502(2019).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 98-690 IN COMPLEX WITH
RP GLUTATHIONE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, AND
RP MUTAGENESIS OF 666-LEU--LEU-690.
RX PubMed=24604199; DOI=10.1126/science.1246729;
RA Srinivasan V., Pierik A.J., Lill R.;
RT "Crystal structures of nucleotide-free and glutathione-bound mitochondrial
RT ABC transporter Atm1.";
RL Science 343:1137-1140(2014).
CC -!- FUNCTION: Performs an essential function in the generation of
CC cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export
CC of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial
CC proteins (PubMed:10406803, PubMed:31040179, PubMed:25006243).
CC Hydrolyzes ATP (PubMed:25006243, PubMed:24604199). Binds glutathione
CC and may function by transporting a glutathione-conjugated iron-sulfur
CC compound (PubMed:24604199, PubMed:25006243, PubMed:31040179).
CC {ECO:0000269|PubMed:10406803, ECO:0000269|PubMed:24604199,
CC ECO:0000269|PubMed:25006243, ECO:0000269|PubMed:31040179}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=109 uM for glutathione disulfide {ECO:0000269|PubMed:25006243};
CC Vmax=27.4 pmol/min/mg enzyme {ECO:0000269|PubMed:25006243};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24604199}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24604199, ECO:0000269|PubMed:7828591}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:24604199, ECO:0000269|PubMed:25006243,
CC ECO:0000269|PubMed:7828591}.
CC -!- DISRUPTION PHENOTYPE: Impairs cytosolic iron-sulfur (Fe-S) cluster
CC assembly and decreases cytosolic tRNA thiolation.
CC {ECO:0000269|PubMed:31040179}.
CC -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; X82612; CAA57938.1; -; Genomic_DNA.
DR EMBL; X81715; CAA57359.1; -; Genomic_DNA.
DR EMBL; Z49212; CAA89134.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10202.1; -; Genomic_DNA.
DR PIR; S54211; S54211.
DR RefSeq; NP_014030.1; NM_001182810.1.
DR PDB; 4MYC; X-ray; 3.06 A; A/B/C=98-690.
DR PDB; 4MYH; X-ray; 3.38 A; A/B/C=98-690.
DR PDB; 7PSL; EM; 3.30 A; A/B=92-690.
DR PDB; 7PSM; EM; 3.40 A; A/B=92-690.
DR PDB; 7PSN; EM; 2.90 A; A/B=92-690.
DR PDBsum; 4MYC; -.
DR PDBsum; 4MYH; -.
DR PDBsum; 7PSL; -.
DR PDBsum; 7PSM; -.
DR PDBsum; 7PSN; -.
DR AlphaFoldDB; P40416; -.
DR SMR; P40416; -.
DR BioGRID; 35481; 100.
DR DIP; DIP-7617N; -.
DR IntAct; P40416; 8.
DR MINT; P40416; -.
DR STRING; 4932.YMR301C; -.
DR TCDB; 3.A.1.210.1; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P40416; -.
DR MaxQB; P40416; -.
DR PaxDb; P40416; -.
DR PRIDE; P40416; -.
DR EnsemblFungi; YMR301C_mRNA; YMR301C; YMR301C.
DR GeneID; 855347; -.
DR KEGG; sce:YMR301C; -.
DR SGD; S000004916; ATM1.
DR VEuPathDB; FungiDB:YMR301C; -.
DR eggNOG; KOG0057; Eukaryota.
DR GeneTree; ENSGT00940000156281; -.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; P40416; -.
DR OMA; VTEWRTH; -.
DR BioCyc; YEAST:G3O-32967-MON; -.
DR Reactome; R-SCE-1369007; Mitochondrial ABC transporters.
DR PRO; PR:P40416; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40416; protein.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IMP:UniProtKB.
DR GO; GO:1902497; P:iron-sulfur cluster transmembrane transport; IMP:UniProtKB.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ion transport; Iron; Iron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..690
FT /note="Iron-sulfur clusters transporter ATM1,
FT mitochondrial"
FT /id="PRO_0000000258"
FT TOPO_DOM 27..110
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT TRANSMEM 111..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..155
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..228
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT TRANSMEM 229..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..340
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT TRANSMEM 341..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..374
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT TRANSMEM 375..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..690
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0000269|PubMed:25006243"
FT DOMAIN 111..401
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 436..672
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 280..284
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0007744|PDB:4MYH"
FT BINDING 343..346
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:24604199,
FT ECO:0007744|PDB:4MYH"
FT BINDING 393
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 469..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 216
FT /note="R->Q: Decreases ATP hydrolysis. Decreases
FT transporter activity."
FT /evidence="ECO:0000269|PubMed:25006243"
FT MUTAGEN 475
FT /note="K->M: Loss of function; significant decrease in ATP-
FT binding; no homodimerization."
FT /evidence="ECO:0000269|PubMed:15225610"
FT MUTAGEN 475
FT /note="Missing: Decreases ATP hydrolysis. Decreases
FT transporter activity."
FT /evidence="ECO:0000269|PubMed:25006243"
FT MUTAGEN 598
FT /note="E->A: Loss of function; slight decrease in ATP-
FT binding."
FT /evidence="ECO:0000269|PubMed:15225610"
FT MUTAGEN 666..690
FT /note="Missing: Impairs protein stability."
FT /evidence="ECO:0000269|PubMed:24604199"
FT CONFLICT 23
FT /note="I -> IRNHS (in Ref. 1; CAA57938)"
FT /evidence="ECO:0000305"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 105..139
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7PSM"
FT HELIX 152..200
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 211..232
FT /evidence="ECO:0007829|PDB:7PSN"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 257..303
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:7PSN"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 314..366
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4MYH"
FT HELIX 372..395
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:4MYC"
FT STRAND 436..443
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:7PSM"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 476..482
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4MYC"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:4MYC"
FT HELIX 539..548
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:7PSN"
FT TURN 559..563
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:4MYC"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 575..589
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 592..598
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 605..616
FT /evidence="ECO:0007829|PDB:7PSN"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 640..646
FT /evidence="ECO:0007829|PDB:7PSN"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:7PSN"
FT HELIX 666..675
FT /evidence="ECO:0007829|PDB:7PSN"
SQ SEQUENCE 690 AA; 77522 MW; 009757811D331343 CRC64;
MLLLPRCPVI GRIVRSKFRS GLIRNHSPVI FTVSKLSTQR PLLFNSAVNL WNQAQKDITH
KKSVEQFSSA PKVKTQVKKT SKAPTLSELK ILKDLFRYIW PKGNNKVRIR VLIALGLLIS
AKILNVQVPF FFKQTIDSMN IAWDDPTVAL PAAIGLTILC YGVARFGSVL FGELRNAVFA
KVAQNAIRTV SLQTFQHLMK LDLGWHLSRQ TGGLTRAMDR GTKGISQVLT AMVFHIIPIS
FEISVVCGIL TYQFGASFAA ITFSTMLLYS IFTIKTTAWR THFRRDANKA DNKAASVALD
SLINFEAVKY FNNEKYLADK YNGSLMNYRD SQIKVSQSLA FLNSGQNLIF TTALTAMMYM
GCTGVIGGNL TVGDLVLINQ LVFQLSVPLN FLGSVYRDLK QSLIDMETLF KLRKNEVKIK
NAERPLMLPE NVPYDITFEN VTFGYHPDRK ILKNASFTIP AGWKTAIVGS SGSGKSTILK
LVFRFYDPES GRILINGRDI KEYDIDALRK VIGVVPQDTP LFNDTIWENV KFGRIDATDE
EVITVVEKAQ LAPLIKKLPQ GFDTIVGERG LMISGGEKQR LAIARVLLKN ARIMFFDEAT
SALDTHTEQA LLRTIRDNFT SGSRTSVYIA HRLRTIADAD KIIVLDNGRV REEGKHLELL
AMPGSLYREL WTIQEDLDHL ENELKDQQEL
