ATPAM_MAIZE
ID ATPAM_MAIZE Reviewed; 508 AA.
AC P05494;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=ATPA;
OS Zea mays (Maize).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16664454; DOI=10.1104/pp.79.2.571;
RA Braun C.J., Levings C.S. III;
RT "Nucleotide sequence of the F1-ATPase alpha subunit from maize
RT mitochondria.";
RL Plant Physiol. 79:571-577(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2900697; DOI=10.1007/bf00365628;
RA Isaac P.G., Brennicke A., Dunbar S.M., Leaver C.J.;
RT "The mitochondrial genome of fertile maize (Zea mays L.) contains two
RT copies of the gene encoding the alpha-subunit of the F1-ATPase.";
RL Curr. Genet. 10:321-328(1985).
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; M16222; AAA70269.1; -; Genomic_DNA.
DR EMBL; Z00026; CAA77319.1; -; Genomic_DNA.
DR PIR; A23757; PWZMAM.
DR RefSeq; XP_008674060.1; XM_008675838.1.
DR AlphaFoldDB; P05494; -.
DR SMR; P05494; -.
DR EnsemblPlants; Zm00001eb434640_T001; Zm00001eb434640_P001; Zm00001eb434640.
DR EnsemblPlants; Zm00001eb437040_T001; Zm00001eb437040_P001; Zm00001eb437040.
DR EnsemblPlants; Zm00001eb442780_T001; Zm00001eb442780_P001; Zm00001eb442780.
DR GeneID; 103650219; -.
DR Gramene; Zm00001eb434640_T001; Zm00001eb434640_P001; Zm00001eb434640.
DR Gramene; Zm00001eb437040_T001; Zm00001eb437040_P001; Zm00001eb437040.
DR Gramene; Zm00001eb442780_T001; Zm00001eb442780_P001; Zm00001eb442780.
DR KEGG; zma:103650219; -.
DR MaizeGDB; 69198; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 470054at2759; -.
DR ExpressionAtlas; P05494; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:AgBase.
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:0051087; F:chaperone binding; IPI:AgBase.
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..508
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000144400"
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 508 AA; 55180 MW; FBA3DD33141A0456 CRC64;
MEFSPRAAEL TTLLESRMIN FYTNLKVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG
VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGK
GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI
AIDTILNQKQ MNSRGTNESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSMLVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSSKLELAQY REVAAFAQFG SDLDAATQAL
LNRGARLTEV PKQPQYEPLP IEKQIVVIYA AVNGFCDRMP LDRISQYEKN ILSTINPELL
KSFLEKGGLT NERKMEPDAS LKESALNL
