ID   B3U2W6_9MAGN            Unreviewed;       457 AA.
AC   B3U2W6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-NOV-2024, entry version 45.
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:ACB57120.1};
OS   Pseuduvaria mollis.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ACB57120.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Annonaceae;
OC   Malmeoideae; Miliuseae; Pseuduvaria.
OX   NCBI_TaxID=513631 {ECO:0000313|EMBL:ACB57120.1};
RN   [1] {ECO:0000313|EMBL:ACB57120.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18436457; DOI=10.1016/j.ympev.2008.03.028;
RA   Su Y.C., Smith G.J., Saunders R.M.;
RT   "Phylogeny of the basal angiosperm genus Pseuduvaria (Annonaceae) inferred
RT   from five chloroplast DNA regions, with interpretation of morphological
RT   character evolution.";
RL   Mol. Phylogenet. Evol. 48:188-206(2008).
RN   [2] {ECO:0000313|EMBL:ACB57120.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Su Y.C.F., Smith G.J.D., Saunders R.M.K.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5-
CC         bisphosphate + CO2 + 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 = 2-phosphoglycolate + (2R)-
CC         3-phosphoglycerate + 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; EU522320; ACB57120.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3U2W6; -.
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   FunFam; 3.20.20.110:FF:000001; Ribulose bisphosphate carboxylase large chain; 1.
DR   FunFam; 3.30.70.150:FF:000001; Ribulose bisphosphate carboxylase large chain; 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:ACB57120.1};
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:ACB57120.1}.
FT   DOMAIN          12..132
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          142..450
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:ACB57120.1"
FT   NON_TER         457
FT                   /evidence="ECO:0000313|EMBL:ACB57120.1"
SQ   SEQUENCE   457 AA;  50887 MW;  908E8090100BC742 CRC64;
     FKAGVKEYKL TYYTPEYETK DTDILAAFRV TPQPGVPPEE AGAAVAAESS TGTWTTVWTD
     GLTSLDRYKG RCYHIEPVAG EENQYIAYVA YPLDLFEEGS VTNMFTSIVG NVFGFKALRA
     LRLEDLRIPT SYIKTFQGPP HGIQVERDKL NKYGRPLLGC TIKPKLGLSA KNYGRAVYEC
     LRGGLDFTKD DENVNSQPFM RWRDRFLFCA EALYKAQAET GEIKGHYLNA TAGTCEEMMK
     RAVFARELGV PIVMHDYLTG GFTANTSLAH YCRDNGLLLH IHRAMHAVID RQKNHGMHFR
     VLAKALRMSG GDHIHAGTVV GKLEGERDIT LGFVDLLRDD FIEKDRSRGI YFTQDWVSLP
     GVLPVASGGI HVWHMPALTE IFGDDSVLQF GGGTLGHPWG NAPGAVANRV ALEACVQARN
     EGRDLARQGN EIIREASKWS PELAAACEVW KEIKFEF
//