ATPAM_ORYSJ
ID ATPAM_ORYSJ Reviewed; 509 AA.
AC P0C522; P15998; Q2F8Z9; Q2F952; Q7JAI5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=ATPA;
OS Oryza sativa subsp. japonica (Rice).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Taichung 65; TISSUE=Shoot;
RX PubMed=2138730; DOI=10.1093/nar/18.5.1302;
RA Kadowaki K., Boireau P., Laporte J.;
RT "Nucleotide sequence of the F1-ATPase alpha subunit gene from rice
RT mitochondria.";
RL Nucleic Acids Res. 18:1302-1302(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RC STRAIN=cv. Nipponbare;
RX PubMed=12471441; DOI=10.1007/s00438-002-0767-1;
RA Notsu Y., Masood S., Nishikawa T., Kubo N., Akiduki G., Nakazono M.,
RA Hirai A., Kadowaki K.;
RT "The complete sequence of the rice (Oryza sativa L.) mitochondrial genome:
RT frequent DNA sequence acquisition and loss during the evolution of
RT flowering plants.";
RL Mol. Genet. Genomics 268:434-445(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16384910; DOI=10.1104/pp.105.070060;
RA Tian X., Zheng J., Hu S., Yu J.;
RT "The rice mitochondrial genomes and their variations.";
RL Plant Physiol. 140:401-410(2006).
RN [4]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 1-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
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 -!- RNA EDITING: Modified_positions=393 {ECO:0000269|PubMed:12471441}, 431
CC {ECO:0000269|PubMed:12471441}, 497 {ECO:0000269|PubMed:12471441}, 500
CC {ECO:0000269|PubMed:12471441};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; X51422; CAA35787.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BA000029; BAC19899.2; -; Genomic_DNA.
DR EMBL; DQ167400; AAZ99349.1; ALT_SEQ; Genomic_DNA.
DR PIR; JQ0411; PWRZAM.
DR RefSeq; YP_002000594.1; NC_011033.1.
DR AlphaFoldDB; P0C522; -.
DR SMR; P0C522; -.
DR STRING; 39947.P0C522; -.
DR PaxDb; P0C522; -.
DR PRIDE; P0C522; -.
DR GeneID; 6450183; -.
DR KEGG; osa:6450183; -.
DR InParanoid; P0C522; -.
DR OrthoDB; 470054at2759; -.
DR Proteomes; UP000059680; Mitochondrion.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IC:Gramene.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW RNA editing; Transport.
FT CHAIN 1..509
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000290117"
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 509 AA; 55373 MW; 93EE049C340C637F CRC64;
MEFSPRAAEL TTLLESRMTN FYTNFQVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG
VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGK
GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI
AIDTILNQKQ MNSRGTNESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSILVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSLKLELAQY REVAAFAQFG SDLDAATQAL
LNRGARLTEV SKQPQYEPLP IEKQIVVIYA AVNGFCDRMP LDRISQYEKA ILSTINPELL
KSFNEKGGLT NERKIELDAF LKQTAKEIN
