ID A5DBB0_PICGU Unreviewed; 612 AA.
AC A5DBB0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000256|ARBA:ARBA00018860};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN ORFNames=PGUG_00565 {ECO:0000313|EMBL:EDK36467.1};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36467.1, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK36467.1, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001741};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00029433}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00029427}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; CH408155; EDK36467.1; -; Genomic_DNA.
DR RefSeq; XP_001487188.1; XM_001487138.1.
DR AlphaFoldDB; A5DBB0; -.
DR STRING; 294746.A5DBB0; -.
DR GeneID; 5128955; -.
DR KEGG; pgu:PGUG_00565; -.
DR VEuPathDB; FungiDB:PGUG_00565; -.
DR eggNOG; KOG1352; Eukaryota.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; A5DBB0; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 5473187at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR NCBIfam; TIGR01042; V-ATPase_V1_A; 1.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 23..85
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 101..223
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 232..457
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 612 AA; 67098 MW; 59A3D781B4B046AF CRC64;
MENARKEVKR LSLDDKEANY GQIFSVSGPV IVAENMIGCA MYELVKVGHD NLVGEVIRIN
ADKATIQVYE ETAGVTVGDP VMRTGKPLSV ELGPGLMENI YDGIQRPLRD IREKADSIYI
PRGIDAPALS RTAKYDFKPA GLKVGDHITG GDIFGSVFEN SLLSDHKILL PPRARGTITS
IAESGSYTVE DTVLEVEFDG KKHSYTMMHT WPVRVPRPVA EKLNADHPLL TGQRVLDSLF
PCVQGGTTCI PGAFGCGKTV ISQSLSKYSN SDNIVYVGCG ERGNEMAEVL MEFPELFTEI
DGRKEPIMKR TTLVANTSNM PVAAREASIY TGITLAEYLR DQGKDVSMIA DSSSRWAEAL
REISGRLGEM PADQGFPAYL GSKLASFYER AGNAVALGSP NRTGSVSIVA AVSPAGGDFS
DPVTTATLGI TQVFWGLDKK LAQRKHFPSI NTAASYSKYT NVLDKYYDEN YPEFATLRNK
IKEMISNAEE LDQVVQLVGK SALSDADKIT LDVANLIKED FLQQNGYSTY DAFCPIWKTY
AMMRAFVLYY DEAQKAVSNG AHWSKLAEET ADIKHAVSSS KFFEPSRGEK EAEKEFGSLL
TRISEKFAEA SE
//
