ATPAM_HELAN
ID ATPAM_HELAN Reviewed; 510 AA.
AC P18260;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=ATPA;
OS Helianthus annuus (Common sunflower).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Baso;
RX PubMed=2143817; DOI=10.1093/nar/18.15.4588;
RA Koehler R.H., Loessel A., Zetsche K.;
RT "Nucleotide sequence of the F1-ATPase alpha subunit gene of sunflower
RT mitochondria.";
RL Nucleic Acids Res. 18:4588-4588(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. CMS89, and cv. HA89;
RX PubMed=2143818; DOI=10.1093/nar/18.15.4599;
RA Siculella L., D'Ambrosio L., de Tuglie A.D., Gallerani R.;
RT "Minor differences in the primary structures of atpA genes coded on the
RT mtDNA of fertile and male sterile sunflower lines.";
RL Nucleic Acids Res. 18:4599-4599(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1714033; DOI=10.1007/bf00273925;
RA Koehler R.H., Horn R., Loessl A., Zetsche K.;
RT "Cytoplasmic male sterility in sunflower is correlated with the co-
RT transcription of a new open reading frame with the atpA gene.";
RL Mol. Gen. Genet. 227:369-376(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-510.
RC STRAIN=cv. Texanus ANT1;
RX PubMed=7858220; DOI=10.1007/bf00019495;
RA Spassova M., Moneger F., Leaver C.J., Petrov P., Atanassov A.,
RA Nijkamp H.J.J., Hille J.;
RT "Characterisation and expression of the mitochondrial genome of a new type
RT of cytoplasmic male-sterile sunflower.";
RL Plant Mol. Biol. 26:1819-1831(1994).
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; X53537; CAA37613.1; -; Genomic_DNA.
DR EMBL; X52838; CAA37022.1; -; Genomic_DNA.
DR EMBL; X55963; CAA39428.1; -; Genomic_DNA.
DR EMBL; X82386; CAA57786.1; -; Genomic_DNA.
DR PIR; S10997; S10997.
DR PIR; S19261; S19261.
DR RefSeq; YP_008999569.1; NC_023337.1.
DR AlphaFoldDB; P18260; -.
DR SMR; P18260; -.
DR PRIDE; P18260; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr14g0628421; CDS:HanXRQr2_Chr14g0628421.1; HanXRQr2_Chr14g0628421.
DR GeneID; 18250974; -.
DR Gramene; mRNA:HanXRQr2_Chr14g0628421; CDS:HanXRQr2_Chr14g0628421.1; HanXRQr2_Chr14g0628421.
DR KEGG; han:18250974; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 470054at2759; -.
DR PhylomeDB; P18260; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; 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; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 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.
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 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; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Transport.
FT CHAIN 1..510
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000144399"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 373
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT VARIANT 228
FT /note="A -> L (in strain: cv. CMS89)"
SQ SEQUENCE 510 AA; 55487 MW; 01CC0EDA5A1E7616 CRC64;
MEFSPRAAEL TTLLESRISN FYTNFQVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG
VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGR
GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI
AIDTILNQKQ MNSRSTSESE TLYCVYVAIG QKRSTVAQLV QILSEANAME YSILVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVIPITD GQICSETELF
YRGIRPAINV GLSVSRVGSA AQLKTMKQVC GSSKLELAQY REVAALAQFG SDLDAATQAL
LNRGARLTEV PKQPQYAPLP IEKQILVIYA AVNGFCDRMP LDRISQYERA ILKSIKTELL
QSLLEKGGLT NERKMEPDTF LKECALPYTI
