ID   RBL_SOLTU               Reviewed;         477 AA.
AC   P25079; Q27S42; Q2VEG9;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Precursor;
GN   Name=rbcL;
OS   Solanum tuberosum (Potato).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16668878; DOI=10.1104/pp.99.1.356;
RA   Enyedi A.J., Pell E.J.;
RT   "Comparison of the rbcL gene sequence of two potato cultivars with
RT   differential sensitivity to ozone.";
RL   Plant Physiol. 99:356-358(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Desiree;
RX   PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA   Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA   Jeong W.-J., Liu J.R.;
RT   "The complete chloroplast genome sequences of Solanum tuberosum and
RT   comparative analysis with Solanaceae species identified the presence of a
RT   241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL   Plant Cell Rep. 25:1369-1379(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Desiree;
RA   Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S., Cardi T.;
RT   "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT   Desiree and comparative analyses with other Solanaceae genomes.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, AND ACETYLATION AT PRO-3.
RX   PubMed=16668742; DOI=10.1104/pp.98.3.1170;
RA   Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.;
RT   "Posttranslational modifications in the amino-terminal region of the large
RT   subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several
RT   plant species.";
RL   Plant Physiol. 98:1170-1174(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   -!- 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   -!- 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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
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 (By similarity). {ECO:0000250}.
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:0000250}.
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' (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M76402; AAB01597.1; -; Genomic_DNA.
DR   EMBL; DQ231562; ABB90049.1; -; Genomic_DNA.
DR   EMBL; DQ386163; ABD47065.1; -; Genomic_DNA.
DR   PIR; PQ0797; PQ0797.
DR   RefSeq; YP_635647.1; NC_008096.2.
DR   AlphaFoldDB; P25079; -.
DR   SMR; P25079; -.
DR   STRING; 4113.P25079; -.
DR   iPTMnet; P25079; -.
DR   PaxDb; 4113-PGSC0003DMT400083063; -.
DR   GeneID; 4099985; -.
DR   KEGG; sot:4099985; -.
DR   eggNOG; ENOG502QTI9; Eukaryota.
DR   InParanoid; P25079; -.
DR   OrthoDB; 1275719at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P25079; baseline.
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: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   1: Evidence at protein level;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Direct protein sequencing; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW   Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT                   /id="PRO_0000031409"
FT   CHAIN           3..477
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000031410"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            334
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT   MOD_RES         14
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT   MOD_RES         201
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        247
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        26
FT                   /note="T -> P (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="R -> S (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="R -> L (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="F -> Y (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="T -> V (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="G -> A (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="N -> S (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="V -> E (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="A -> C (in Ref. 1; AAB01597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   477 AA;  52944 MW;  46E2EC09C2619F72 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMLTSI
     VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQA ETGEIKGHYL
     NATAGTCEEM MKRAVFAREL GTPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFIEQDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVKA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIVFNFA AMDVLDK
//

ID   A0A0N7CI26_SOLTU        Unreviewed;       477 AA.
AC   A0A0N7CI26;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 45.
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,
GN   ECO:0000313|EMBL:AKM22039.1};
OS   Solanum tuberosum (Potato).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AKM22039.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EMBL:AKM22039.1};
RN   [1] {ECO:0000313|EMBL:AKM22039.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cho K.-S., Kim K.-H., Yang T.-J.;
RT   "To survey the complete chloroplast genome of Solanum tuberosum.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QJH90239.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TBR {ECO:0000313|EMBL:QJH90239.1};
RX   PubMed=31893289; DOI=10.1007/s00122-019-03519-6;
RA   Kyriakidou M., Achakkagari S.R., Galvez Lopez J.H., Zhu X., Tang C.Y.,
RA   Tai H.H., Anglin N.L., Ellis D., Stromvik M.V.;
RT   "Complete plastome assemblies from a panel of 13 diverse potato taxa.";
RL   Theor. Appl. Genet. 133:951-e0240124(2020).
RN   [3] {ECO:0000313|EMBL:QNS39220.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tai H.;
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:QQL03478.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pedrueza M., Oh B., Zhang J., Rahman M., Pokharel A., Tuladhar R., Koag M.,
RA   Wang C., Lee R., Kubin G., Bonser J.D.;
RL   Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QNS39220.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=33763586;
RA   Achakkagari S.R., Tai H.H., Davidson C., Jong H., Stromvik M.V.;
RT   "The complete plastome sequences of nine diploid potato clones.";
RL   Mitochondrial DNA B Resour 6:811-813(2021).
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|ARBA:ARBA00025888, ECO:0000256|HAMAP-
CC       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; KM489056; AKM22039.1; -; Genomic_DNA.
DR   EMBL; MT120865; QJH90239.1; -; Genomic_DNA.
DR   EMBL; MT511702; QNS39220.1; -; Genomic_DNA.
DR   EMBL; MT511703; QNS39306.1; -; Genomic_DNA.
DR   EMBL; MT511704; QNS39392.1; -; Genomic_DNA.
DR   EMBL; MT511708; QNS39736.1; -; Genomic_DNA.
DR   EMBL; MT511709; QNS39822.1; -; Genomic_DNA.
DR   EMBL; MW307946; QQL03478.1; -; Genomic_DNA.
DR   EMBL; MW307947; QQL03565.1; -; Genomic_DNA.
DR   EMBL; MW307948; QQL03652.1; -; Genomic_DNA.
DR   EMBL; MW307949; QQL03739.1; -; Genomic_DNA.
DR   RefSeq; YP_635647.1; NC_008096.2.
DR   AlphaFoldDB; A0A0N7CI26; -.
DR   SMR; A0A0N7CI26; -.
DR   GeneID; 4099985; -.
DR   KEGG; sot:4099985; -.
DR   OrthoDB; 1275719at2759; -.
DR   ExpressionAtlas; A0A0N7CI26; baseline.
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: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, 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:AKM22039.1};
KW   Disulfide bond {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_01338,
KW   ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AKM22039.1}.
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;  52944 MW;  46E2EC09C2619F72 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMLTSI
     VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQA ETGEIKGHYL
     NATAGTCEEM MKRAVFAREL GTPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFIEQDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVKA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIVFNFA AMDVLDK
//