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ATPA_DICDI
ID   ATPA_DICDI              Reviewed;         519 AA.
AC   Q9XPJ9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=atp1; ORFNames=DDB_G0294012;
OS   Dictyostelium discoideum (Slime mold).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=10821186; DOI=10.1007/pl00008685;
RA   Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA   Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT   "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT   content and genome organization.";
RL   Mol. Gen. Genet. 263:514-519(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 6-14; 171-180 AND 292-298, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V., Veltman D.M., Insall R.H.;
RL   Submitted (JAN-2010) to UniProtKB.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AB000109; BAA78060.1; -; Genomic_DNA.
DR   PIR; T43756; T43756.
DR   RefSeq; NP_050078.1; NC_000895.1.
DR   AlphaFoldDB; Q9XPJ9; -.
DR   SMR; Q9XPJ9; -.
DR   GeneID; 2193895; -.
DR   KEGG; ddi:DidioMp11; -.
DR   dictyBase; DDB_G0294012; atp1.
DR   InParanoid; Q9XPJ9; -.
DR   OMA; LQAPGVM; -.
DR   PhylomeDB; Q9XPJ9; -.
DR   PRO; PR:Q9XPJ9; -.
DR   Proteomes; UP000002195; Mitochondrion.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
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   GO; GO:0009617; P:response to bacterium; IDA:dictyBase.
DR   GO; GO:0046688; P:response to copper ion; IDA:dictyBase.
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   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   Transport.
FT   CHAIN           1..519
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000312371"
FT   BINDING         188..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            382
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   519 AA;  57237 MW;  D4856399C917E4B1 CRC64;
     MQLEKMLTEV NIERSKFNTY NVLLQYIKAV TQKYNLNKVS SKYGKVLFIK DGVVKVSGLS
     QIKIGEKVEF VGKNLYGMAL NLEATSVGIV IFGEDTAIYE GVIVKRCEQN FAIKVDKTML
     GRVVDVLGQP IDGLGELKDT KTTRVMSVER KAPGIVTRKS VHESMLTGVK IVDALLPIGR
     GQRELIIGDR QTGKSAIAVD AILNQQVNKD IVCIYVAVGQ KKSTVRRLVE MLNTKGALEY
     TIVVVSTASD AAPLQFLAPY TGCTIGEYFR DEGKHALIVY DDLSKHAVAY RQMSLLLRRP
     PGREAYPGDV FYIHSRLLER AAKLNEKYGC GSLTAFPIVE TQAGDVSAYI PTNIISITDG
     QIFLEKELFN KGIRPAVNVG LSVSRVGSAA QSAVMKKLAG ALKLELAQYR ELARFEQFSS
     NADAVTTQIL KKGKLTIELL KQVNNNPMSI GLEALMIYAM GTSYFQNLDL SLVRSEETKL
     LNYINSIASF KLYAACVDAV KAFNPKDTVF AEMCQSYVK
 
 
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