ATPAM_OENBI
ID ATPAM_OENBI Reviewed; 511 AA.
AC P05492;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=ATPA;
OS Oenothera biennis (German evening primrose) (Onagra biennis).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX NCBI_TaxID=3942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schuster W., Brennicke A.;
RT "Pseudocopies of the ATPase alpha-subunit gene in Oenothera mitochondria
RT are present on different circular molecules.";
RL Mol. Gen. Genet. 204:29-35(1986).
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; X04023; CAA27656.1; -; Genomic_DNA.
DR PIR; S07316; S07316.
DR AlphaFoldDB; P05492; -.
DR SMR; P05492; -.
DR PRIDE; P05492; -.
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..511
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000144402"
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"
SQ SEQUENCE 511 AA; 55597 MW; 91992AAAEDB7B316 CRC64;
MEFSPRAAEL TTLLESRITN FYTNFQVDEI GRVISVGDGI ARVYGLNEIQ AGEMVEFASG
VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKSLLGRVV DALGVPIDGR
GALGDHERRR VEVKVPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI
AIDTILNQKQ MNSRATSESE TLYCVYVAIG QKRSTVAQLV QILSEGNALE YSILVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSLKLELAQY REVAAFAQFG SDLDAATQAL
LNRGARLTEI LKQPQYAPLP IEKQIIVIYA AVNGFCDRMP LDRISQYERA IPQSVKQELL
QSLVEKGGLN NERKIEPDAF LKENAKPYIK G