ID   A0A344X9G4_9LAMI        Unreviewed;       416 AA.
AC   A0A344X9G4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   19-JAN-2022, entry version 12.
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:AXE75480.1};
OS   Salvia cavaleriei var. cavaleriei.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AXE75480.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC   Salvia; Salvia incertae sedis.
OX   NCBI_TaxID=1208401 {ECO:0000313|EMBL:AXE75480.1};
RN   [1] {ECO:0000313|EMBL:AXE75480.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29945172;
RA   Hu G.X., Takano A., Drew B.T., Liu E.D., Soltis D.E., Soltis P.S., Peng H.,
RA   Xiang C.L.;
RT   "Phylogeny and staminal evolution of Salvia (Lamiaceae, Nepetoideae) in
RT   East Asia.";
RL   Ann. Bot. 0:0-0(2018).
RN   [2] {ECO:0000313|EMBL:AXE75480.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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         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|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       disulfide-linked. The disulfide link is formed within the large subunit
CC       homodimers. {ECO:0000256|ARBA:ARBA00025888}.
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; MG823791; AXE75480.1; -; Genomic_DNA.
DR   EMBL; MG823792; AXE75481.1; -; Genomic_DNA.
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 {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:AXE75480.1};
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:AXE75480.1}.
FT   DOMAIN          6..126
FT                   /note="RuBisCO_large_N"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          136..413
FT                   /note="RuBisCO_large"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AXE75480.1"
FT   NON_TER         416
FT                   /evidence="ECO:0000313|EMBL:AXE75480.1"
SQ   SEQUENCE   416 AA;  46191 MW;  BD036ABAA6E6D678 CRC64;
     EYKLTYYTPE YETKDTDILA AFRVTPQPGV PPEEAGAAVA AESSTGTWTT VWTDGLTSLD
     RYKGRCYHIE PVPGEKDQYI CYVAYPLDLF EEGSVTNMFT SIVGNVFGFK ALRALRLEDL
     RIPVAYVKTF QGPPHGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD
     FTKDDENVNS QPFMRWRDRF LFCAEAIYKA QTETGEIKGH YLNATAGTCE EMMKRAIFAR
     ELGVPIVMHD YLTGGFTANT TLAHYCRDNG LLLHIHRAMH AVIDRQKNHG MHFRVLAKAL
     RLSGGDHIHA GTVVGKLEGE RDITLGFVDL LRDDFVEKDR SRGIYFTQDW VSLPGVIPVA
     SGGIHVWHMP ALTEIFGDDS VLQFGGGTLG HPWGNAPGAV ANRVAVEACV QARNEG
//