ID   A0A344X9G4_9LAMI        Unreviewed;       416 AA.
AC   A0A344X9G4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-FEB-2019, entry version 4.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
DE            EC=4.1.1.39 {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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae;
OC   Mentheae; Salvia; Salvia unplaced.
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.,
RA   Peng H., Xiang C.L.;
RT   "Phylogeny and staminal evolution of Salvia (Lamiaceae, Nepetoideae)
RT   in 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 3-phospho-D-glycerate + 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|RuleBase:RU000302};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC         Evidence={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.
CC       {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.
CC       {ECO:0000256|RuleBase:RU000302}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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|RuleBase:RU000302};
KW   Carbon dioxide fixation {ECO:0000256|RuleBase:RU000302};
KW   Chloroplast {ECO:0000256|RuleBase:RU000302,
KW   ECO:0000313|EMBL:AXE75480.1}; Lyase {ECO:0000256|RuleBase:RU000302};
KW   Magnesium {ECO:0000256|RuleBase:RU000302};
KW   Metal-binding {ECO:0000256|RuleBase:RU000302};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000302};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000302};
KW   Photorespiration {ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000313|EMBL:AXE75480.1}.
FT   DOMAIN        6    126       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      136    413       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AXE75480.1}.
FT   NON_TER     416    416       {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
//