ADT_MYCTT
ID ADT_MYCTT Reviewed; 315 AA.
AC G2QNH0;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=ADP/ATP translocase {ECO:0000305};
DE AltName: Full=ADP/ATP carrier {ECO:0000303|PubMed:30611538};
DE Short=TtAac {ECO:0000303|PubMed:30611538};
GN ORFNames=MYCTH_2316753 {ECO:0000312|EMBL:AEO62043.1};
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2] {ECO:0007744|PDB:6GCI}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT LYS-302 IN COMPLEX WITH
RP BONGKREKIC ACID AND CARDIOLIPIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-30; ARG-88; ASN-96;
RP ARG-100; GLY-192; ILE-193; TYR-196; ARG-197; SER-238; ARG-246; ARG-287 AND
RP GLN-302.
RX PubMed=30611538; DOI=10.1016/j.cell.2018.11.025;
RA Ruprecht J.J., King M.S., Zoegg T., Aleksandrova A.A., Pardon E.,
RA Crichton P.G., Steyaert J., Kunji E.R.S.;
RT "The molecular mechanism of transport by the mitochondrial ADP/ATP
RT carrier.";
RL Cell 176:435-447(2019).
CC -!- FUNCTION: ADP:ATP antiporter that mediates import of ADP into the
CC mitochondrial matrix for ATP synthesis, and export of ATP out to fuel
CC the cell (PubMed:30611538). Cycles between the cytoplasmic-open state
CC (c-state) and the matrix-open state (m-state): operates by the
CC alternating access mechanism with a single substrate-binding site
CC intermittently exposed to either the cytosolic (c-state) or matrix (m-
CC state) side of the inner mitochondrial membrane (PubMed:30611538).
CC {ECO:0000269|PubMed:30611538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:30611538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000269|PubMed:30611538};
CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by
CC the membrane-permeable bongkrekic acid (BKA) (PubMed:30611538). The
CC cytoplasmic-open state (c-state) is inhibited by the membrane-
CC impermeable toxic inhibitor carboxyatractyloside (CATR)
CC (PubMed:30611538). {ECO:0000269|PubMed:30611538}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30611538}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30611538}.
CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC the membrane, but cross the membrane at an angle. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000269|PubMed:30611538}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; CP003008; AEO62043.1; -; Genomic_DNA.
DR RefSeq; XP_003667288.1; XM_003667240.1.
DR PDB; 6GCI; X-ray; 3.30 A; A=1-315.
DR PDBsum; 6GCI; -.
DR AlphaFoldDB; G2QNH0; -.
DR SMR; G2QNH0; -.
DR STRING; 78579.XP_003667288.1; -.
DR ABCD; G2QNH0; 1 sequenced antibody.
DR EnsemblFungi; AEO62043; AEO62043; MYCTH_2316753.
DR GeneID; 11509839; -.
DR KEGG; mtm:MYCTH_2316753; -.
DR VEuPathDB; FungiDB:MYCTH_2316753; -.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; G2QNH0; -.
DR OrthoDB; 870903at2759; -.
DR Proteomes; UP000007322; Chromosome 7.
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:0005471; F:ATP:ADP antiporter activity; IDA:UniProtKB.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IDA:UniProtKB.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IDA:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45635; PTHR45635; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..315
FT /note="ADP/ATP translocase"
FT /id="PRO_0000452326"
FT TOPO_DOM 1..13
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT TOPO_DOM 38..80
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT TOPO_DOM 105..115
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT TOPO_DOM 146..184
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT TOPO_DOM 214..216
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT TOPO_DOM 243..283
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 284..304
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT TOPO_DOM 305..315
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT REPEAT 13..106
FT /note="Solcar"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 118..210
FT /note="Solcar"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 218..304
FT /note="Solcar"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT MOTIF 245..250
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 30
FT /ligand="bongkrekate"
FT /ligand_id="ChEBI:CHEBI:178020"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 62
FT /ligand="a cardiolipin"
FT /ligand_id="ChEBI:CHEBI:62237"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 81..83
FT /ligand="a cardiolipin"
FT /ligand_id="ChEBI:CHEBI:62237"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 88..89
FT /ligand="bongkrekate"
FT /ligand_id="ChEBI:CHEBI:178020"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 88
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P18238"
FT BINDING 96
FT /ligand="bongkrekate"
FT /ligand_id="ChEBI:CHEBI:178020"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 166
FT /ligand="a cardiolipin"
FT /ligand_id="ChEBI:CHEBI:62237"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 184..185
FT /ligand="a cardiolipin"
FT /ligand_id="ChEBI:CHEBI:62237"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 196..197
FT /ligand="bongkrekate"
FT /ligand_id="ChEBI:CHEBI:178020"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 245
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P18238"
FT BINDING 260..261
FT /ligand="a cardiolipin"
FT /ligand_id="ChEBI:CHEBI:62237"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT BINDING 280..282
FT /ligand="a cardiolipin"
FT /ligand_id="ChEBI:CHEBI:62237"
FT /evidence="ECO:0000269|PubMed:30611538,
FT ECO:0007744|PDB:6GCI"
FT MUTAGEN 30
FT /note="K->A: Abolished ADP:ATP antiporter activity.
FT Decreased bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 88
FT /note="R->A: Abolished ADP:ATP antiporter activity.
FT Decreased bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 96
FT /note="N->A: Decreased bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 100
FT /note="R->A: Strongly decreased ADP:ATP antiporter
FT activity."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 192
FT /note="G->A: Abolished ADP:ATP antiporter activity."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 193
FT /note="I->A: Strongly decreased ADP:ATP antiporter
FT activity. Decreased bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 196
FT /note="Y->A: Abolished ADP:ATP antiporter activity.
FT Decreased bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 197
FT /note="R->A: Abolished ADP:ATP antiporter activity.
FT Decreased bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 238
FT /note="S->A: Decreased ADP:ATP antiporter activity. Does
FT not affect bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 246
FT /note="R->A: Abolished ADP:ATP antiporter activity."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 287
FT /note="R->A: Strongly decreased ADP:ATP antiporter
FT activity. Does not affect bongkrekic acid-binding."
FT /evidence="ECO:0000269|PubMed:30611538"
FT MUTAGEN 302
FT /note="Q->K: Increased thermal stability."
FT /evidence="ECO:0000269|PubMed:30611538"
FT HELIX 14..44
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 82..107
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 116..156
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6GCI"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 186..211
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 221..249
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6GCI"
FT HELIX 285..305
FT /evidence="ECO:0007829|PDB:6GCI"
SQ SEQUENCE 315 AA; 34000 MW; 757B5BC978E67FE1 CRC64;
MSNKQETKIL GMPPFVVDFL MGGVSAAVSK TAAAPIERIK LLVQNQDEMI KAGRLDRRYN
GIIDCFRRTT ADEGLMALWR GNTANVIRYF PTQALNFAFR DKFKAMFGYK KDKDGYAKWM
AGNLASGGAA GATSLLFVYS LDYARTRLAN DAKSAKGGGA RQFNGLIDVY RKTLASDGIA
GLYRGFGPSV AGIVVYRGLY FGMYDSIKPV VLVGPLANNF LASFLLGWCV TTGAGIASYP
LDTVRRRMMM TSGEAVKYKS SIDAFRQIIA KEGVKSLFKG AGANILRGVA GAGVLSIYDQ
LQILLFGKAF KGGSG
