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RBL_PACAQ
ID   RBL_PACAQ               Reviewed;         469 AA.
AC   Q9XQJ6;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 88.
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: Fragment;
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Pachira aquatica (Guiana chestnut).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Bombacoideae; Pachira.
OX   NCBI_TaxID=69118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Bayer C., Fay M.F., de Bruin A.Y., Savolainen V., Morton C.M., Kubitzki K.,
RA   Alverson W.S., Chase M.W.;
RT   "Support for an expanded family concept of Malvaceae within a
RT   recircumscribed oder Malvales: a combined analysis of plastid atpB and rbcL
RT   DNA sequences.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AJ233119; CAB44247.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XQJ6; -.
DR   SMR; Q9XQJ6; -.
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; -; 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   Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase;
KW   Photorespiration; Photosynthesis; Plastid.
FT   CHAIN           <1..>469
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062554"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         194
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         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            327
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         7
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         194
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   DISULFID        240
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   NON_TER         1
FT   NON_TER         469
SQ   SEQUENCE   469 AA;  52073 MW;  1D4E8B7C28EA6B4E CRC64;
     KASVGFKAGV KEYKLTYYTP EYEVKDTDIL AAFRVTPQPG VPPEEAGAAV AAESSTGTWT
     TVWTDGLTSL DRYKGRCYHI EPVAGEENQY ICYVAYPLDL FEEGSVTNMF TSIVGNVFGF
     KALRALRLED LRIPTSYTKT FQGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENVN SQPFMRWRDR FVFCAEAIYK AQAETGEIKG HYLNATAGTC
     EEMMKRAIFA RELGVPIVMH DYLTGGFTAN TSLAHYCRDN GLLLHIHRAM HAVIDRQKNH
     GMHFRVLAKA LRLSGGDHIH AGTVVGKLEG ERDITLGFVD LLRDDFIEKD RSRGIYFTQD
     WVSLPGVLPV ASGGIHVWHM PALTEIFGDD SVLQFGGGTL GHPWGNAPGA VANRVALEAC
     VKARNEGRDL AREGNEIIRE ASKWSPELAA ACEVWKEIKF EFQAVDTLD
 
 
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