ID A0A1J0PCY9_9SYNE Unreviewed; 470 AA.
AC A0A1J0PCY9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338};
GN Name=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
GN Synonyms=rbcL {ECO:0000256|HAMAP-Rule:MF_01338};
GN ORFNames=BM449_13870 {ECO:0000313|EMBL:APD49127.1};
OS Synechococcus sp. SynAce01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1916956 {ECO:0000313|EMBL:APD49127.1, ECO:0000313|Proteomes:UP000182608};
RN [1] {ECO:0000313|Proteomes:UP000182608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SynAce01 {ECO:0000313|Proteomes:UP000182608};
RA Tang J., Daroch M., Liang Y., Jiang D., Shah M.;
RL Submitted (NOV-2016) 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};
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|HAMAP-Rule:MF_01338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01338};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|ARBA:ARBA00023587,
CC ECO:0000256|HAMAP-Rule:MF_01338}.
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; CP018091; APD49127.1; -; Genomic_DNA.
DR RefSeq; WP_071801780.1; NZ_CP018091.1.
DR AlphaFoldDB; A0A1J0PCY9; -.
DR STRING; 1916956.BM449_13870; -.
DR KEGG; syny:BM449_13870; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000182608; Chromosome.
DR GO; GO:0031470; C:carboxysome; 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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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 Bacterial microcompartment {ECO:0000256|ARBA:ARBA00024446};
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 Carboxysome {ECO:0000256|ARBA:ARBA00023669, ECO:0000256|HAMAP-
KW Rule:MF_01338};
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}; Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338};
KW Reference proteome {ECO:0000313|Proteomes:UP000182608}.
FT DOMAIN 16..136
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 146..454
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 115
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 193
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 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT SITE 326
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 193
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
SQ SEQUENCE 470 AA; 52442 MW; 7A3C6F64F58787E7 CRC64;
MSKKFDAGVK EYRDTYWTPD YVPLDTDLLA CFKVTGQDGV PREEVAAAVA AESSTGTWSA
VWSELLTDLD FYKGRCYRIE DVPGDKESFY AFVAYPLDLF EEGSVTNVLT SLVGNVFGFK
ALRHLRLEDI RFPMAFIKTC PGPPNGICVE RDRMNKYGRP LLGCTIKPKL GLSGKNYGRV
VYECLRGGLD FTKDDENINS QPFQRWQNRF EFVAEAVESA QQETGEKKGH YLNCTAATPE
EMYERAEFAK ELGQPIIMHD YITGGFTANT GLSKWCRKNG MLLHIHRAMH AVIDRHPKHG
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGFIDQ LRESFIPEDR SRGNFFDQDW
GSMPGVFAVA SGGIHVWHMP ALVAIFGDDS VLQFGGGTHG HPWGSAAGAA ANRVALEACV
KARNAGREIE KESRDILMEA AKHSPELAIA LETWKEIKFE FDTVDKLDVN
//
