ID E5DK96_9ROSI Unreviewed; 349 AA.
AC E5DK96;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
DE Flags: Fragment;
GN Name=atp1 {ECO:0000313|EMBL:ADL63214.1};
OS Karrabina biagiana.
OG Mitochondrion {ECO:0000313|EMBL:ADL63214.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cunoniaceae; Karrabina.
OX NCBI_TaxID=133501 {ECO:0000313|EMBL:ADL63214.1};
RN [1] {ECO:0000313|EMBL:ADL63214.1}
RP NUCLEOTIDE SEQUENCE.
RA Qiu Y.-L., Li L., Wang B., Xue J., Hendry T.A., Li R., Brown J.W., Liu Y.,
RA Hudson G.T., Chen Z.;
RT "Angiosperm phylogeny inferred from sequences of four mitochondrial
RT genes.";
RL Zhi Wu Fen Lei Xue Bao 48:391-425(2010).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; GU351025; ADL63214.1; -; Genomic_DNA.
DR AlphaFoldDB; E5DK96; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 3.40.50.12240; -; 1.
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; PF02874; ATP-synt_ab_N; 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|RuleBase:RU003551};
KW ATP-binding {ECO:0000256|RuleBase:RU003551};
KW CF(1) {ECO:0000256|RuleBase:RU003551};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:ADL63214.1};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003551};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..44
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 101..325
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADL63214.1"
FT NON_TER 349
FT /evidence="ECO:0000313|EMBL:ADL63214.1"
SQ SEQUENCE 349 AA; 37408 MW; 6401C8889729A0DB CRC64;
AGEMVEFASG VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV
DALGVPIDGR GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKALDSLVP IGRGQRELII
GDRQTGKTAI AIDTILNQKQ MNSRATSESE TLYCVYVAIG QKRSTVAQLV QILSEANALE
YSILVAATAS DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR
PPGREAFPGD VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVIPITD
GQICLETELF YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSSKLELAQ
//
