ID Q32682_9VIRI Unreviewed; 451 AA.
AC Q32682;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 22-FEB-2023, entry version 100.
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:AAA84903.1};
OS Nitellopsis obtusa.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAA84903.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Nitellopsis.
OX NCBI_TaxID=40811 {ECO:0000313|EMBL:AAA84903.1};
RN [1] {ECO:0000313|EMBL:AAA84903.1}
RP NUCLEOTIDE SEQUENCE.
RA McCourt R.M., Karol K.G., Guerlesquin M., Feist M.;
RT "Phylogeny of extant genera in the family Characeae (Charales,
RT Charophyceae) based on rbcL sequences and morphology.";
RL Am. J. Bot. 83:125-131(1996).
RN [2] {ECO:0000313|EMBL:AAX39486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KGK0057e {ECO:0000313|EMBL:AAX39486.1};
RA Karol K.G.;
RT "Estimating divergence times in the Charophyta.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAA84903.1}
RP NUCLEOTIDE SEQUENCE.
RA Karol K.G.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AQY72483.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KGK2013 {ECO:0000313|EMBL:AQY72483.1};
RA Perez W., Casanova M.T., Hall J.D., McCourt R.M., Karol K.G.;
RT "Phylogenetic congruence of ribosomal operon and plastid gene sequences for
RT the Characeae with an emphasis on Tolypella (Characeae, Charophyceae).";
RL Phycologia 56:230-237(2017).
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 {ECO:0000256|RuleBase:RU000302}.
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; U27530; AAA84903.1; -; Genomic_DNA.
DR EMBL; AY823702; AAX39486.1; -; Genomic_DNA.
DR EMBL; KX431022; AQY72483.1; -; Genomic_DNA.
DR AlphaFoldDB; Q32682; -.
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:AAA84903.1};
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, ECO:0000313|EMBL:AAA84903.1}.
FT DOMAIN 15..135
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 145..451
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:AAA84903.1"
FT NON_TER 451
FT /evidence="ECO:0000313|EMBL:AAA84903.1"
SQ SEQUENCE 451 AA; 49856 MW; E0508D83D2DE024B CRC64;
GTGFKAGVKD YRLTYYTPEY KTKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV
WTDGLTSLDR YKGRCYDIEP VAGEENQYIA YVAYPLDLFE EGSVTNLFTS IVGNVFGFKA
LRALRLEDLR IPPAYIKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FVTEAIYKSQ AETGEIKGHY LNATAGTCEE
MLKRAQCARE LGVPIIMHDY LTGGFTANTT LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM
HFRVLAKALR LSGGDHVHSG TVVGKLEGER EVTLGFVDLL RDDYIEKDRS RGVYFTQDWV
SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ
ARNEGRDLAR EGNEIIREAA KWSPELAAAC E
//
