ID ATPA_DICDI Reviewed; 519 AA.
AC Q9XPJ9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=atp1; ORFNames=DDB_G0294012;
OS Dictyostelium discoideum (Social amoeba).
OG Mitochondrion.
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=10821186; DOI=10.1007/pl00008685;
RA Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT content and genome organization.";
RL Mol. Gen. Genet. 263:514-519(2000).
RN [2]
RP PROTEIN SEQUENCE OF 6-14; 171-180 AND 292-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits. Subunit
CC alpha does not bear the catalytic high-affinity ATP-binding sites (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AB000109; BAA78060.1; -; Genomic_DNA.
DR PIR; T43756; T43756.
DR RefSeq; NP_050078.1; NC_000895.1.
DR AlphaFoldDB; Q9XPJ9; -.
DR SMR; Q9XPJ9; -.
DR STRING; 44689.Q9XPJ9; -.
DR GeneID; 2193895; -.
DR KEGG; ddi:DidioMp11; -.
DR dictyBase; DDB_G0294012; atp1.
DR InParanoid; Q9XPJ9; -.
DR OMA; INQRDNW; -.
DR PhylomeDB; Q9XPJ9; -.
DR PRO; PR:Q9XPJ9; -.
DR Proteomes; UP000002195; Mitochondrion.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IDA:dictyBase.
DR GO; GO:0046688; P:response to copper ion; IDA:dictyBase.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transport.
FT CHAIN 1..519
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000312371"
FT BINDING 188..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 382
FT /note="Required for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 519 AA; 57237 MW; D4856399C917E4B1 CRC64;
MQLEKMLTEV NIERSKFNTY NVLLQYIKAV TQKYNLNKVS SKYGKVLFIK DGVVKVSGLS
QIKIGEKVEF VGKNLYGMAL NLEATSVGIV IFGEDTAIYE GVIVKRCEQN FAIKVDKTML
GRVVDVLGQP IDGLGELKDT KTTRVMSVER KAPGIVTRKS VHESMLTGVK IVDALLPIGR
GQRELIIGDR QTGKSAIAVD AILNQQVNKD IVCIYVAVGQ KKSTVRRLVE MLNTKGALEY
TIVVVSTASD AAPLQFLAPY TGCTIGEYFR DEGKHALIVY DDLSKHAVAY RQMSLLLRRP
PGREAYPGDV FYIHSRLLER AAKLNEKYGC GSLTAFPIVE TQAGDVSAYI PTNIISITDG
QIFLEKELFN KGIRPAVNVG LSVSRVGSAA QSAVMKKLAG ALKLELAQYR ELARFEQFSS
NADAVTTQIL KKGKLTIELL KQVNNNPMSI GLEALMIYAM GTSYFQNLDL SLVRSEETKL
LNYINSIASF KLYAACVDAV KAFNPKDTVF AEMCQSYVK
//
