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Database: UniProt
Entry: Q9SCE1_9ROSI
LinkDB: Q9SCE1_9ROSI
Original site: Q9SCE1_9ROSI 
ID   Q9SCE1_9ROSI            Unreviewed;       466 AA.
AC   Q9SCE1;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   22-FEB-2023, entry version 77.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:CAB65013.1};
OS   Fagonia cretica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Zygophyllales; Zygophyllaceae; Zygophylloideae; Fagonia.
OX   NCBI_TaxID=90528 {ECO:0000313|EMBL:CAB65013.1};
RN   [1] {ECO:0000313|EMBL:CAB65013.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:CAB65013.1};
RX   AGRICOLA=IND22293563;
RA   Sheahan M.C., Chase M.W.;
RT   "Phylogenetic relationships within Zygophyllaceae based on DNA sequences of
RT   three plastid regions, with special emphasis on Zygophylloideae.";
RL   Syst. Bot. 25:371-384(2000).
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};
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR   EMBL; AJ133855; CAB65013.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9SCE1; -.
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; 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   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAB65013.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT   DOMAIN          15..135
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          145..453
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:CAB65013.1"
SQ   SEQUENCE   466 AA;  51573 MW;  996F9ED850657002 CRC64;
     SVGFKAGVKD YKLTYYTPEY ETKDTDILAA FRVSPQPGVP PEEAGAAVAA ESSTGTWTAV
     WTDGLTSLDR YKGRCYNLEA VPGEDNQYIA YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA
     LRALRLEDLR IPTAYTKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
     YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEAIYKAQ AETGEIKGHY LNATAGTCEE
     MMKRAACARE LGVPIVMHDY LTGGFTANTT LAHYCRDNGL LLHIHRAMHA VIDRQKNHGI
     HFRVLAKALR MSGGDHIHAG TVVGKLEGER EITLGFVDLL RDDFIEKDRS RGIYFTQDWV
     SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ
     ARNEGRDLAR EGNIIIREAS KWSPELAAAC EIWKEIKFEF PAMDTL
//
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