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RBL_QUERU
ID   RBL_QUERU               Reviewed;         475 AA.
AC   Q01874;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE   Flags: Precursor;
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Quercus rubra (Northern red oak) (Quercus borealis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Fagaceae; Quercus.
OX   NCBI_TaxID=3512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1502205; DOI=10.1073/pnas.89.16.7844;
RA   Bousquet J., Strauss S.H., Doerksen A.H., Price R.A.;
RT   "Extensive variation in evolutionary rate of rbcL gene sequences among seed
RT   plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7844-7848(1992).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
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:0000255|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
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:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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:0000255|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:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR   EMBL; M58391; AAA82699.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01874; -.
DR   SMR; Q01874; -.
DR   PRIDE; Q01874; -.
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; -; 1.
DR   Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation;
KW   Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT                   /id="PRO_0000031383"
FT   CHAIN           3..475
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000031384"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            334
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         3
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         14
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         201
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   DISULFID        247
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ   SEQUENCE   475 AA;  52601 MW;  B25F2EF416C1950A CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYHTPDYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEENQFIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PTSYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGIH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDYIEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFP AMDTL
 
 
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