ID Q5SBW7_9POAL Unreviewed; 477 AA.
AC Q5SBW7;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 88.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|HAMAP-Rule:MF_01338};
GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338};
OS Restio similis.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAV53407.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Restionaceae; Restio.
OX NCBI_TaxID=136747 {ECO:0000313|EMBL:AAV53407.1};
RN [1] {ECO:0000313|EMBL:AAV53407.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16012098; DOI=10.1080/10635150590923317;
RA Hardy C.R., Linder H.P.;
RT "Intraspecific variability and timing in ancestral ecology reconstruction:
RT a test case from the cape flora.";
RL Syst. Biol. 54:299-316(2005).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site.
CC {ECO:0000256|HAMAP-Rule:MF_01338}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01338, 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|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01338,
CC ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01338,
CC 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|HAMAP-Rule:MF_01338}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204, ECO:0000256|HAMAP-
CC Rule:MF_01338}.
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DR EMBL; AY690746; AAV53407.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5SBW7; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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:SF12; 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, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:AAV53407.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01338}; Methylation {ECO:0000256|HAMAP-Rule:MF_01338};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AAV53407.1}.
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..462
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 14
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
SQ SEQUENCE 477 AA; 52976 MW; B44C65618F8CE9CD CRC64;
MSPQTETKAS VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV VGEENQYIAY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PPSYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE MTLGFVDLLR DDFIEKDRSR
GIFFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVQA RNEGRDLARE GNEVIREACK WSPELAAACE VWKAIKFEFE PVDKLDK
//
