ATM1_DEBHA
ID ATM1_DEBHA Reviewed; 696 AA.
AC Q6BXD7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=DEHA2B03894g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382134; CAG85125.2; -; Genomic_DNA.
DR RefSeq; XP_457132.2; XM_457132.1.
DR AlphaFoldDB; Q6BXD7; -.
DR SMR; Q6BXD7; -.
DR STRING; 4959.XP_457132.2; -.
DR EnsemblFungi; CAG85125; CAG85125; DEHA2B03894g.
DR GeneID; 2913198; -.
DR KEGG; dha:DEHA2B03894g; -.
DR VEuPathDB; FungiDB:DEHA2B03894g; -.
DR eggNOG; KOG0057; Eukaryota.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q6BXD7; -.
DR OMA; VTEWRTH; -.
DR OrthoDB; 248727at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
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..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 68..696
FT /note="Iron-sulfur clusters transporter ATM1,
FT mitochondrial"
FT /id="PRO_0000255444"
FT TOPO_DOM 68..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, 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..696
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 438..674
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 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 471..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 696 AA; 77475 MW; B052D8AA8F45A07F CRC64;
MIKWGLFGAV KPFRSMVPLS QTRSLIISKS SLVRSKRVST IRPQLAPVNP YSKIYGRRFF
SSSHKLGVNT KEDSSTYLFG RKISTSESKM LKSLLVTIWP KNKPSFKLRV IFALSLLIAS
KLLNVEVPFF FKKIIDEMNV DWNDQLGTVG TVIGTLIIAY GGARFGAVLF GELRNAVFAS
VAQTAIKRVA HNTFVHLLNM DLNFHLSRQT GGLTRAIDRG TKGISYVLNA MVFHIIPISF
EISMVCGILI YNYGLSFAAV TLATMLSYSV FTIKTTAWRT GFRRQANNAD NQAATVALDS
LLNYESVKYF NNEGFQASKY NTALTNYQNA SVKVATSLAY LNAGQNFIFT SALTAMMYMG
CNGVATGSLT VGDLVLINQL VFQLSVPLSF LGSVYRELKQ SLLDMENLFQ LQNHEIKIKD
ASNAKPLLLN STGVPGEIKF ENVTFGYHPD RPILQNASFT IPAGEKIAIV GPSGSGKSTI
LRLIFRFYDV ESGKIFIDGQ DISKVTVESL RRSIGIVPQD TPLFNDTILE NIRYGRLDAT
DKEIHEMIDK VQLTKLIEDS PNGVNTIVGE RGMMISGGEK QRLAIARLLL KRAPITLFDE
ATSALDTHTE QSLLRTIRKV LTKKANTHIA IAHRLRTIAD ADKIIVLNKG QVQEEGTHHN
LLQNPNSLYS QLWNIQENLD IDEELNEYAK ETEEQK
