ID F8QMH5_9FLOR Unreviewed; 488 AA.
AC F8QMH5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302};
GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338};
OS Cumathamnion decipiens.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADI87180.1}.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Delesseriaceae; Cumathamnion.
OX NCBI_TaxID=131060 {ECO:0000313|EMBL:ADI87180.1};
RN [1] {ECO:0000313|EMBL:ADI87180.1}
RP NUCLEOTIDE SEQUENCE.
RA Carlile A.L., Waaland J.R.;
RT "Molecular Systematics of North Pacific Ceramiaceae (Ceramiales,
RT Rhodophyta) Species.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|ARBA:ARBA00011371, ECO:0000256|HAMAP-Rule:MF_01338,
CC ECO:0000256|RuleBase:RU000302}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}.
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|HAMAP-Rule:MF_01338}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01338}.
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DR EMBL; GQ252546; ADI87180.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QMH5; -.
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: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:ADI87180.1};
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};
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|HAMAP-Rule:MF_01338,
KW ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01338,
KW ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ADI87180.1}.
FT DOMAIN 28..148
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 158..465
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 127
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 205
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 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT SITE 337
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 205
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
SQ SEQUENCE 488 AA; 54286 MW; E2ADB80B2D4247F2 CRC64;
MSNSVEERTR IKNERYESGV IPYAKMGYWD PNYVIKETDV LSLFRVTPQP GVDPVEASAA
VAGESSTATW TVVWTDLLTA CDLYRAKAYK VDAVPNTSDQ YFAYIAYDID LFEEGSIANL
TASIIGNVFG FKAVKALRLE DMRMPVAYLK TFQGPATGIV VERERMDKFG RPFLGATVKP
KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWKE RFLYSMEAVN RSIAASGEVK
GHYMNVTAAT MEDMYERAEF AKDLGTVIIM VDLVIGYTAI QSMAIWSRKN DMILHLHRAG
NSTYSRQKIH GMNFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMIKGFYN TLLLPYLETN
LPQGIFFQQD WAALRKVTPV ASGGIHCGQM HQLLDYLGND VVLQFGGGTI GHPDGIQAGA
TANRVALESM VIARNEMRDY VTEGPQILRD AAKTCGPLQT ALDLWKDISF NYTSTDTADF
VETPTANV
//
