ID A0A3B6JHJ0_WHEAT Unreviewed; 509 AA.
AC A0A3B6JHJ0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4D02G137800.1.cds1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS4D02G137800.1.cds1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4D02G137800.1.cds1};
RA Rossello M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4D02G137800.1.cds1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) 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.
CC {ECO:0000256|ARBA:ARBA00037296}.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003551}.
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. {ECO:0000256|ARBA:ARBA00011648}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004273}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
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DR AlphaFoldDB; A0A3B6JHJ0; -.
DR SMR; A0A3B6JHJ0; -.
DR STRING; 4565.A0A3B6JHJ0; -.
DR EnsemblPlants; TraesCS4D02G137800.1; TraesCS4D02G137800.1.cds1; TraesCS4D02G137800.
DR Gramene; TraesARI4D03G02496660.1; TraesARI4D03G02496660.1.CDS1; TraesARI4D03G02496660.
DR Gramene; TraesCS4D02G137800.1; TraesCS4D02G137800.1.cds1; TraesCS4D02G137800.
DR Gramene; TraesJUL4D03G02477000.1; TraesJUL4D03G02477000.1.CDS1; TraesJUL4D03G02477000.
DR Gramene; TraesLAC4D03G02411120.1; TraesLAC4D03G02411120.1.CDS1; TraesLAC4D03G02411120.
DR Gramene; TraesLDM4D03G02460140.1; TraesLDM4D03G02460140.1.CDS1; TraesLDM4D03G02460140.
DR Gramene; TraesMAC4D03G02456170.1; TraesMAC4D03G02456170.1.CDS1; TraesMAC4D03G02456170.
DR Gramene; TraesPARA_EIv1.0_1436180.1; TraesPARA_EIv1.0_1436180.1.CDS1; TraesPARA_EIv1.0_1436180.
DR Gramene; TraesSYM4D03G02485400.1; TraesSYM4D03G02485400.1.CDS1; TraesSYM4D03G02485400.
DR OMA; KAMRGCV; -.
DR Proteomes; UP000019116; Chromosome 4D.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; 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 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 FunFam; 1.20.150.20:FF:000001; ATP synthase subunit alpha; 1.
DR FunFam; 2.40.30.20:FF:000001; ATP synthase subunit alpha; 1.
DR FunFam; 3.40.50.300:FF:002432; ATP synthase subunit alpha, mitochondrial; 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 NCBIfam; NF009884; PRK13343.1; 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 PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 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 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003551};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003551};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003551};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU000339};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000339}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003551};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 27..94
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 151..375
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 382..492
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 509 AA; 55524 MW; 5D649F6D067B9016 CRC64;
MEFSPRAAEL TTLLESRMTN FYTNFQVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG
VKGIALNLEN ENVGIVVFGS DTAIKEGDLV MRTGSIVDVP AGKAMLGRVV DALGVPIDGK
GALSDHERRR VEVKVPGMIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII RDRQTGKTAI
AIDTILNQKQ MNSRGTNESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSILVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHTLII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSSTALPMI ETQAGDVSAY IPTNVISITD GQICLEIELF
YRGIRPAINV GLSISRVGSA AQLKAMKQVC GSSKLELAQY RQVAAFAQFG SDLDAATQAL
LNRGARLTEV PKQPQYEPLP IEKQIVVIYA AVNGFCDRLP LDRISQYEKA ILSTINPELQ
KSFLEKGGLT NERKMEPDAS LKESTLPYL
//
