ATM1_ASHGO
ID ATM1_ASHGO Reviewed; 691 AA.
AC Q751N2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000305};
DE EC=7.-.-.- {ECO:0000250|UniProtKB:Q2G506};
DE Flags: Precursor;
GN Name=ATM1 {ECO:0000305}; OrderedLocusNames=AGL335W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). Hydrolyzes ATP (By similarity). Binds
CC glutathione and may function by transporting a glutathione-conjugated
CC iron-sulfur compound (By similarity). {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
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; AE016820; AAS54156.1; -; Genomic_DNA.
DR RefSeq; NP_986332.1; NM_211394.1.
DR AlphaFoldDB; Q751N2; -.
DR SMR; Q751N2; -.
DR STRING; 33169.AAS54156; -.
DR PRIDE; Q751N2; -.
DR EnsemblFungi; AAS54156; AAS54156; AGOS_AGL335W.
DR GeneID; 4622625; -.
DR KEGG; ago:AGOS_AGL335W; -.
DR eggNOG; KOG0057; Eukaryota.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q751N2; -.
DR OMA; VTEWRTH; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
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; IEA:EnsemblFungi.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..691
FT /note="Iron-sulfur clusters transporter ATM1,
FT mitochondrial"
FT /id="PRO_0000255437"
FT TOPO_DOM 23..109
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 132..154
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 155..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 179..227
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 228..251
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 252
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 274..339
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 340..358
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 359..373
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 396..691
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 110..400
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 435..671
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 279..283
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 342..345
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 392
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 468..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 691 AA; 76821 MW; 908631BA33F69B64 CRC64;
MFRLLRFSPS RYYPRSMAPV RWSTHPYHVT APRMWGTRMP LQLQASLRPN NAVEKGISGD
VKVAGAMVKP AASGGESAKS KTPTVSELKI LKDLFRYIWP RGDRKVKTRV LIALGLLLGS
KLLNVQVPFF FKSTVDSMNI EWGDVGTALP IAVTLTVLSY GAARFGAVLF VELRNAVFSN
VAQSAITKVS LQTFQHLMKL DLGWHLSRQT GGLTRAMDRG CKGISYVLSA MVFHIIPITF
EISMVCGILT YQFGASFAAI TFSTMLLYSI FTFRTTAWRT RFRRDANKAD NKAASVALDS
LINFEAVKYF NNEKYLADKY HTSLMKYRDS QIKVSQSLAF LNTGQNLIFT TALTAMMYMA
CNGVMQGSLT VGDLVLINQL VFQLSVPLNF LGSVYRDLKQ SLIDMESLFK LQKNQVTIKN
SPNAQNLPIH KPLDIRFENV TFGYDPERRI LNNVSFTIPA GMKTAIVGPS GSGKSTILKL
VFRFYEPEQG RILVGGTDIR DLDLLSLRKA IGVVPQDTPL FNDTIWENVK FGNISSSDDE
ILRAIEKAQL TKLLQNLPKG ASTVVGERGL MISGGEKQRL AIARVLLKDA PLMFFDEATS
ALDTHTEQAL LHTIQQNFSS NSKTSVYVAH RLRTIADADK IIVLEQGSVR EEGTHSSLLA
SQGSLYRGLW DIQENLTLPE RPEQSTGSQH A
