ID A0A2H4WZB2_9GENT Unreviewed; 509 AA. AC A0A2H4WZB2; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 24-JAN-2024, entry version 18. DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551}; GN Name=atp1 {ECO:0000313|EMBL:AUD38672.1}; OS Lasianthus sp. Kainulaninen et al. 17. OG Mitochondrion {ECO:0000313|EMBL:AUD38672.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Lasiantheae; OC Lasianthus. OX NCBI_TaxID=1406727 {ECO:0000313|EMBL:AUD38672.1}; RN [1] {ECO:0000313|EMBL:AUD38672.1} RP NUCLEOTIDE SEQUENCE. RA Rydin C., Wikstrom N., Bremer B.; RT "Conflicting results from mitochondrial genomic data challenge current RT views of Rubiaceae phylogeny."; RL Am. J. Bot. 104:1522-1532(2017). 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 ECO:0000256|RuleBase:RU004287}. 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, ECO:0000256|RuleBase:RU000339}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KY638137; AUD38672.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2H4WZB2; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. 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; 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:SF8; ATP SYNTHASE SUBUNIT ALPHA-RELATED; 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|RuleBase:RU000342, ECO:0000313|EMBL:AUD38672.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU003551}; 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..494 FT /note="ATP synthase alpha subunit C-terminal" FT /evidence="ECO:0000259|Pfam:PF00306" SQ SEQUENCE 509 AA; 55285 MW; EF1F3386546D8E98 CRC64; MELYPRAAEL TSLLESRISN FYTNLKVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGR GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI AIDTILNQKQ MNSRATSESE TLYCVYVAIG QKRSTVAQLV QIISEANALE YSILVAATAS DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVIPITD GQICLETELF YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSSKLELAQY REVAAFAQFG SDLDAATQAL LNRGARLTEV PKQPQYTPLP IEKQILVIYA AVNGFCDRMP LDKIAQYERV LPNSVKPELL QSFLEKGGLT NERKIEPDSF LKESALAFI //