ATPAM_SOYBN
ID ATPAM_SOYBN Reviewed; 508 AA.
AC Q01915; M1FPH1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=ATPA; Synonyms=atp1-1, atp1-2, atp1-3;
GN ORFNames=GlmaxMp39, GlmaxMp55, GlmaxMp78;
OS Glycine max (Soybean) (Glycine hispida).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Williams 82; TISSUE=Hypocotyl;
RX PubMed=8435853; DOI=10.1007/bf00351502;
RA Chanut F.A., Grabau E.A., Gesteland R.F.;
RT "Complex organization of the soybean mitochondrial genome: recombination
RT repeats and multiple transcripts at the atpA loci.";
RL Curr. Genet. 23:234-247(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Aiganhuang; TISSUE=Etiolated seedling;
RX PubMed=23431381; DOI=10.1371/journal.pone.0056502;
RA Chang S., Wang Y., Lu J., Gai J., Li J., Chu P., Guan R., Zhao T.;
RT "The mitochondrial genome of soybean reveals complex genome structures and
RT gene evolution at intercellular and phylogenetic levels.";
RL PLoS ONE 8:E56502-E56502(2013).
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; Z14031; CAA78407.1; -; Genomic_DNA.
DR EMBL; JX463295; AFR34317.1; -; Genomic_DNA.
DR EMBL; JX463295; AFR34321.1; -; Genomic_DNA.
DR EMBL; JX463295; AFR34327.1; -; Genomic_DNA.
DR PIR; S29792; S29792.
DR RefSeq; YP_007516887.1; NC_020455.1.
DR RefSeq; YP_007516904.1; NC_020455.1.
DR RefSeq; YP_007516927.1; NC_020455.1.
DR AlphaFoldDB; Q01915; -.
DR SMR; Q01915; -.
DR PRIDE; Q01915; -.
DR ProMEX; Q01915; -.
DR GeneID; 15308543; -.
DR GeneID; 15308608; -.
DR GeneID; 15308624; -.
DR KEGG; gmx:15308543; -.
DR KEGG; gmx:15308608; -.
DR KEGG; gmx:15308624; -.
DR InParanoid; Q01915; -.
DR OrthoDB; 470054at2759; -.
DR Proteomes; UP000008827; Mitochondrion.
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); 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 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 Reference proteome; Transport.
FT CHAIN 1..508
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000144408"
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; 55331 MW; C70C73CC3C6D314F CRC64;
MEFSVRAAEL TTLLESRITN FYTNFQVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG
VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGR
GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI
AIDTILNQKQ MNSRATSESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSILVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSLKLELAQY REVAAFAQFG SDLDAATQAL
LNRGARLTEV LKQPQYAPLP IEKQILVIYA AVNGFCDRMP LDKIPQYERD ILTTIKPELL
QSLKGGLTSE RKIELEKFLK EKGGTYYI
