CFXQ_CYAM1
ID CFXQ_CYAM1 Reviewed; 293 AA.
AC O22025;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 98.
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 CfxQ homolog {ECO:0000305};
GN Name=Rca {ECO:0000303|PubMed:27872295}; Synonyms=cfxQ {ECO:0000305};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ohta N., Sato N., Ueda K., Kuroiwa T.;
RT "Analysis of a plastid gene cluster reveals a close relationship between
RT Cyanidioschyzon and Cyanidium.";
RL J. Plant Res. 110:235-245(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
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 nuclear-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22821.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D63675; BAA22821.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB002583; BAC76109.1; -; Genomic_DNA.
DR RefSeq; NP_848947.1; NC_004799.1.
DR AlphaFoldDB; O22025; -.
DR SMR; O22025; -.
DR STRING; 45157.CMV015CT; -.
DR EnsemblPlants; CMV015CT; CMV015CT; CMV015C.
DR GeneID; 844875; -.
DR Gramene; CMV015CT; CMV015CT; CMV015C.
DR KEGG; cme:CymeCp015; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_008749_1_0_1; -.
DR Proteomes; UP000007014; Chloroplast.
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; 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.
DR TIGRFAMs; TIGR02880; cbbX_cfxQ; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Reference proteome.
FT CHAIN 1..293
FT /note="Ribulose bisphosphate carboxylase/oxygenase
FT activase, chloroplastic"
FT /id="PRO_0000063038"
FT BINDING 75..82
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 reduces activase
FT activity 5-fold."
FT /evidence="ECO:0000269|PubMed:27872295"
FT MUTAGEN 137
FT /note="E->Q: Abolishes ATPase activity and slightly reduces
FT activase activity."
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: Reduces ATPase activity 2-fold and activase
FT activity 8-fold."
FT /evidence="ECO:0000269|PubMed:27872295"
FT CONFLICT 207
FT /note="E -> G (in Ref. 1; BAA22821)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="R -> S (in Ref. 1; BAA22821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 33588 MW; E11EE4DCA5215DD5 CRC64;
MSVQTSQQTV NLQTEFKQTQ IQEVLDDLDR ELIGLQTVKT RIREIAALLL VDRLRQKLGL
SSSNPGLHMS FTGSPGTGKT TVARKMADIL YRLGYIKKGH LITVTRDDLV GQYIGHTAPK
TKQVLKNAMG GVLFIDEAYY LYRPDNERDY GAEAIEILLQ VMENQRDDLV IIFAGYKDKM
DRFYTSNPGL ASRVANHVNF PDYTPEELLM IGKIMLQEQQ YQMTPEAEKV FLQYIQRRME
QPHFANARSV RNALDRARLR QANRIFATPG KKLTKFDLVT IQAEDILKSR LFQ
