ID Q5S845_9MAGN Unreviewed; 460 AA.
AC Q5S845;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 68.
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:AAV65263.1};
OS Guatteria multivenia.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAV65263.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Annonaceae;
OC Annonoideae; Guatterieae; Guatteria.
OX NCBI_TaxID=295175 {ECO:0000313|EMBL:AAV65263.1};
RN [1] {ECO:0000313|EMBL:AAV65263.1}
RP NUCLEOTIDE SEQUENCE.
RA Erkens R.H.J.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAV65263.1}
RP NUCLEOTIDE SEQUENCE.
RA Pirie M.D., Chatrou L.W., Erkens R.H.J., Maas J.W., van der Niet T.,
RA Mols J.B., Richardson J.E.;
RT "Phylogeny reconstruction and molecular dating in four Neotropical genera
RT of Annonaceae: the effect of taxon sampling in age estimations.";
RL (In) Bakker F.T., Chatrou L.W., Gravendeel B., Pelser P.B. (eds.);
RL REGNUM VEGETABILE 143: PLANT SPECIES-LEVEL SYSTEMATICS: NEW PERSPECTIVES ON
RL PATTERN AND PROCESS, pp.149-174, A. R. G. Gantner Verlag, Liechtenstein
RL (2005).
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 {ECO:0000256|RuleBase:RU000302}.
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; AY740987; AAV65263.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5S845; -.
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 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:AAV65263.1};
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:AAV65263.1}.
FT DOMAIN 8..128
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 138..446
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:AAV65263.1"
FT NON_TER 460
FT /evidence="ECO:0000313|EMBL:AAV65263.1"
SQ SEQUENCE 460 AA; 51255 MW; 85ED61074789F743 CRC64;
VKEYKLTYYT PEYETKDTDI LAAFRVTPQP GVPPEEAGAA VAAESSTGTW TTVWTDGLTS
LDRYKGRCYH IEPVVGEENQ YIAYVAYPLD LFEEGSVTNM FTSIVGNVFG FKALRALRLE
DLRIPTAYIK TFQGPPHGIQ VERDKLNKYG RPLLGCTIKP KLGLSAKNYG RAVYECLRGG
LDFTKDDENV NSQPFMRWRD RFLFCAEALF KAQAETGEIK GHYLNATAGT CEEMMKRAVF
ARELGVPIVM HDYLTGGFTA NTTLAHYCRD NGLLLHIHRA MHAVIDRQKN HGMHFRVLAK
ALRMSGGDHI HAGTVVGKLE GERDITLGFV DLLRDDYIEK DRSRGVFFTQ DWVSLPGVIP
VASGGIHVWH MPALTEIFGD DSVLQFGGGT LGHPWGNAPG AVANRVALEA CVQARNEGRD
LARQGNEIIR EASKWSPELA AACEVWKEIK FEFEAMDTLD
//
