ID   ATPA_NEUCR              Reviewed;         551 AA.
AC   P37211; Q7RVM9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE   Flags: Precursor;
GN   Name=atp-1; ORFNames=NCU02514;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1351018; DOI=10.1016/0378-1119(92)90569-b;
RA   Bowman E.J., Knock T.E.;
RT   "Structures of the genes encoding the alpha and beta subunits of the
RT   Neurospora crassa mitochondrial ATP synthase.";
RL   Gene 114:157-163(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; M84191; AAA33560.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA36409.1; -; Genomic_DNA.
DR   PIR; JC1111; JC1111.
DR   RefSeq; XP_965645.1; XM_960552.3.
DR   AlphaFoldDB; P37211; -.
DR   SMR; P37211; -.
DR   STRING; 5141.EFNCRP00000001937; -.
DR   PRIDE; P37211; -.
DR   EnsemblFungi; EAA36409; EAA36409; NCU02514.
DR   GeneID; 3881843; -.
DR   KEGG; ncr:NCU02514; -.
DR   VEuPathDB; FungiDB:NCU02514; -.
DR   HOGENOM; CLU_010091_2_1_1; -.
DR   InParanoid; P37211; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
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; Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..551
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000002431"
FT   BINDING         210..217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            411
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   551 AA;  59522 MW;  FF7AB951FD1E794B CRC64;
     MFRNALRQST RAVGAFSATG RVAARNAAPV VSAVQARTYA DAKATPTEVS SILEQRIRGV
     QEESNLAETG RVLSVGDGIA RVHGMANVQA EELVEFASGV KGMCMNLEAG QVGVVLFGSD
     RLVKEGETVK RTGEIVDVPV GPELLGRVID ALGNPIDGKG PINCKEKRRA QLKAPGILPR
     QSVNQPVQTG LKSVDAMVPI GRGQRELIIG DRQTGKTAVA LDAILNQKRW NSGSDEDKKL
     YCVYVAVGQK RSTVAQLVKT LEENDAMKYS IVVAATASEA APLQYLAPFT GACVGEYFRD
     NGKHSLVIFD DLTKQAVAYR QMSLLLRRPP GREAYPGDVF YLHSRLLERA AKMNKTHGGG
     SMTALPVIET QGGDVSAYIP TNVISITDGQ IFLESELFYK GVRPAINVGL SVSRVGSAAQ
     LKAMKQVAGS LKLFLAQYRE VAAFAQFGSD LDAATKQTLN RGERLTELLK QKQYSPMAVN
     EMVPLIFAGV NGFLDSVPVA KILQWEADFL AHLKTNEPEI MATIDKEGAI SKDLEAKLRD
     VIQTFTKSFL G