ID Q8MA96_9EUKA Unreviewed; 405 AA.
AC Q8MA96;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 22-FEB-2023, entry version 76.
DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:AAM62092.1};
OS Pavlova gyrans.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAM62092.1}.
OC Eukaryota; Haptista; Haptophyta; Pavlovales; Pavlovaceae; Pavlova.
OX NCBI_TaxID=44452 {ECO:0000313|EMBL:AAM62092.1};
RN [1] {ECO:0000313|EMBL:AAM62092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP 607 {ECO:0000313|EMBL:AAM62092.1};
RX PubMed=12172008; DOI=10.1073/pnas.172234799;
RA Yoon H.S., Hackett J.D., Bhattacharya D.;
RT "A single origin of the peridinin- and fucoxanthin-containing plastids in
RT dinoflagellates through tertiary endosymbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11724-11729(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC ChEBI:CHEBI:58272; EC=4.1.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00001067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272; Evidence={ECO:0000256|ARBA:ARBA00000537};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AY119784; AAM62092.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MA96; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 4: Predicted;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Chloroplast {ECO:0000313|EMBL:AAM62092.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AAM62092.1}.
FT DOMAIN 2..77
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 88..394
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAM62092.1"
FT NON_TER 405
FT /evidence="ECO:0000313|EMBL:AAM62092.1"
SQ SEQUENCE 405 AA; 45136 MW; 225844164469BF13 CRC64;
VVWTDLLTAC DLYRAKAFRV DPVPNSSDQY FAYIAYDIDL FEEGSLANLT ASIIGNVFGF
KAVKALRLED MRIPYAYLKT FQGPATGVIV ERERMDKFGR PLLGATVKPK LGLSGKNYGR
VVYEGLKGGL DFLKDDENIN SQPFMRWRER FLFSMEGVNR AAAASGEVKG HYLNSTAATM
EEMYERAEYA KNLGSIIVMI DLVIGYTAIQ SMALWARKHD TILHLHRAGN STYSRQKNHG
MNFRVICKWM RMSGVDHIHA GTVVGKLEGD PLMVKGFYNT LLENKTDINL PEGLFFEQDW
ASLRKCMPVA SGGIHCGQMH QLINYLGDDV VLQFGGGTIG HPDGIQAGAT ANRVALECMV
LARNEGRDYI SEGPQILRDA ARTCGPLQTA LDLWKDITFN YTSTD
//
