CBBX_CYAM1
ID CBBX_CYAM1 Reviewed; 307 AA.
AC M1UXG8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic {ECO:0000303|PubMed:27872295};
DE Short=RuBisCO activase {ECO:0000303|PubMed:27872295};
DE AltName: Full=Protein CbbX homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=Rca {ECO:0000303|PubMed:27872295};
GN Synonyms=CbbX {ECO:0000303|PubMed:18506097};
GN ORFNames=CYME_CMT172C {ECO:0000312|EMBL:BAM83166.1};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=15071595; DOI=10.1038/nature02398;
RA Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA Kuroiwa T.;
RT "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT merolae 10D.";
RL Nature 428:653-657(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT "A 100%-complete sequence reveals unusually simple genomic features in the
RT hot-spring red alga Cyanidioschyzon merolae.";
RL BMC Biol. 5:28-28(2007).
RN [3]
RP FUNCTION.
RX PubMed=18506097; DOI=10.1266/ggs.83.135;
RA Fujita K., Tanaka K., Sadaie Y., Ohta N.;
RT "Functional analysis of the plastid and nuclear encoded CbbX proteins of
RT Cyanidioschyzon merolae.";
RL Genes Genet. Syst. 83:135-142(2008).
RN [4]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-79; TYR-113; GLU-137; ARG-193 AND
RP ARG-238.
RX PubMed=27872295; DOI=10.1073/pnas.1610758113;
RA Loganathan N., Tsai Y.C., Mueller-Cajar O.;
RT "Characterization of the heterooligomeric red-type rubisco activase from
RT red algae.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:14019-14024(2016).
CC -!- FUNCTION: Required for the expression of ribulose 1,5-bisphosphate
CC carboxylase/oxygenase (RuBisCo) (PubMed:18506097). ATPase involved in
CC the activation of red-type RuBisCo, which tends to form inactive
CC complexes with its substrate ribulose 1,5-bisphosphate (RuBP)
CC (PubMed:27872295). Catalyzes the release of RuBP from inhibited RuBisCo
CC in an ATP-dependent manner (PubMed:27872295). Activation of RuBisCO
CC involves the ATP-dependent carboxylation of the epsilon-amino group of
CC lysine leading to a carbamate structure (PubMed:27872295). The nuclear-
CC encoded subunit plays a more critical role in activase function than
CC the plastidial-encoded subunit (PubMed:27872295).
CC {ECO:0000269|PubMed:18506097, ECO:0000269|PubMed:27872295}.
CC -!- SUBUNIT: Forms homooligomers (PubMed:27872295). Forms heterohexameric
CC rings with the plastid-encoded Rca subunit consisting of 3 of each
CC nuclear- and plastidial-encoded subunits that alternate in the ring
CC (PubMed:27872295). {ECO:0000269|PubMed:27872295}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR EMBL; AP006502; BAM83166.1; -; Genomic_DNA.
DR RefSeq; XP_005539202.1; XM_005539145.1.
DR AlphaFoldDB; M1UXG8; -.
DR SMR; M1UXG8; -.
DR STRING; 45157.CMT172CT; -.
DR EnsemblPlants; CMT172CT; CMT172CT; CMT172C.
DR GeneID; 16997649; -.
DR Gramene; CMT172CT; CMT172CT; CMT172C.
DR KEGG; cme:CYME_CMT172C; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_008749_1_3_1; -.
DR OrthoDB; 935713at2759; -.
DR Proteomes; UP000007014; Chromosome 20.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041627; AAA_lid_6.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000470; CbxX/CfqX_mono.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17866; AAA_lid_6; 1.
DR PRINTS; PR00819; CBXCFQXSUPER.
DR PRINTS; PR00820; CBXXCFQX.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..307
FT /note="Ribulose bisphosphate carboxylase/oxygenase
FT activase, chloroplastic"
FT /id="PRO_0000447711"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 79
FT /note="K->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:27872295"
FT MUTAGEN 113
FT /note="Y->A: Increases ATPase activity and abolishes
FT activase activity."
FT /evidence="ECO:0000269|PubMed:27872295"
FT MUTAGEN 137
FT /note="E->Q: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:27872295"
FT MUTAGEN 193
FT /note="R->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:27872295"
FT MUTAGEN 238
FT /note="R->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:27872295"
SQ SEQUENCE 307 AA; 34607 MW; 6A7E7C98CCE554B8 CRC64;
MSIPDDKEAG TIDEFLQKEG VLDILQKLDH DLVGLKPVKD RVREIAALLV VDKLRSRLGL
TGTTPSLHMA FTGSPGTGKT TVAMRMGQIL KAMGYSRSGH LIVATRDDLV GQYVGHTAPK
TKEVIKRAFG GVLFIDEAYY LYNAANDRDY GVEAIEILLN VMEEQREDLV VIFAGYEDRM
NKFYSYIPGI SSRIGNHISF PDYTLEELVD IAKVMVRDME YRIADDAIPA CRAYIEKRMQ
MPYFSNARTV RNLINRARMR SAIRIFNKAM DPNADGLVSR DELMTLITED FPTVQELLER
GETAIVE
