ID O78360_9AQUA Unreviewed; 448 AA.
AC O78360;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|RuleBase:RU000302};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|RuleBase:RU000302};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:CAA67283.1};
OS Ilex rugosa.
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAA67283.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Aquifoliales; Aquifoliaceae; Ilex.
OX NCBI_TaxID=53212 {ECO:0000313|EMBL:CAA67283.1};
RN [1] {ECO:0000313|EMBL:CAA67283.1}
RP NUCLEOTIDE SEQUENCE.
RA Manen J.F., Cuenoud P., Matinez M.D.P.;
RT "Intralineage variation in the pattern of rbcL nucleotide substitution.";
RL Plant Syst. Evol. 211:103-112(1998).
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 ECO:0000256|RuleBase:RU000302};
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 ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers. {ECO:0000256|ARBA:ARBA00025888}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR EMBL; X98733; CAA67283.1; -; Genomic_DNA.
DR AlphaFoldDB; O78360; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd08212; RuBisCO_large_I; 1.
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 HAMAP; MF_01338; RuBisCO_L_type1; 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 InterPro; IPR020888; RuBisCO_lsuI.
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; SFLDG01052; RuBisCO; 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 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567,
KW ECO:0000256|RuleBase:RU000302};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU000302};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:CAA67283.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000302};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000302};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000302};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238,
KW ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 24..144
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 154..440
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 448
FT /evidence="ECO:0000313|EMBL:CAA67283.1"
SQ SEQUENCE 448 AA; 49522 MW; B4F06F109F463D03 CRC64;
MSPQTETKAS VGFKAGVKDY KLNYYTPDYV TKDTDILAAF RVSPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYQIEPV AGEENQFIAY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL
NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKGLRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVKA RNEGRDLARE GNEIIREA
//
