RBL_SYNY3
ID RBL_SYNY3 Reviewed; 470 AA.
AC P54205;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338,
GN ECO:0000303|PubMed:11859847}; OrderedLocusNames=slr0009;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8219082; DOI=10.1007/bf00019295;
RA Amichay D., Levitz R., Gurevitz M.;
RT "Construction of a Synechocystis PCC6803 mutant suitable for the study of
RT variant hexadecameric ribulose bisphosphate carboxylase/oxygenase
RT enzymes.";
RL Plant Mol. Biol. 23:465-476(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=11859847; DOI=10.1007/s004250100638;
RA So A.K., John-McKay M., Espie G.S.;
RT "Characterization of a mutant lacking carboxysomal carbonic anhydrase from
RT the cyanobacterium Synechocystis PCC6803.";
RL Planta 214:456-467(2002).
RN [5]
RP INTERACTION WITH CCMM, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17993516; DOI=10.1128/jb.01283-07;
RA Cot S.S., So A.K., Espie G.S.;
RT "A multiprotein bicarbonate dehydration complex essential to carboxysome
RT function in cyanobacteria.";
RL J. Bacteriol. 190:936-945(2008).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
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 (By similarity). RuBisCO interacts with the C-terminus of
CC CcmM, and can be found in complexes that also include carbonic
CC anhydrase (ccaA). RuBisCO associates with both the internal and shell
CC portion of carboxysomes (PubMed:17993516). {ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000269|PubMed:17993516}.
CC -!- INTERACTION:
CC P54205; P52231: trxA; NbExp=3; IntAct=EBI-862277, EBI-862916;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|PubMed:11859847, ECO:0000269|PubMed:17993516}. Note=This
CC cyanobacterium makes beta-type carboxysomes (PubMed:17993516). In the
CC carboxysome RuBisCO is organized into a paracrystalline array (By
CC similarity). {ECO:0000250|UniProtKB:Q31NB3,
CC ECO:0000269|PubMed:17993516}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; X65960; CAA46773.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10190.1; -; Genomic_DNA.
DR PIR; S39561; S39561.
DR AlphaFoldDB; P54205; -.
DR SMR; P54205; -.
DR IntAct; P54205; 4.
DR STRING; 1148.1001563; -.
DR PaxDb; P54205; -.
DR PRIDE; P54205; -.
DR EnsemblBacteria; BAA10190; BAA10190; BAA10190.
DR KEGG; syn:slr0009; -.
DR eggNOG; COG1850; Bacteria.
DR InParanoid; P54205; -.
DR OMA; IHGHPDG; -.
DR PhylomeDB; P54205; -.
DR BioCyc; MetaCyc:MON-750; -.
DR BRENDA; 4.1.1.39; 382.
DR SABIO-RK; P54205; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
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 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 1: Evidence at protein level;
KW Bacterial microcompartment; Calvin cycle; Carbon dioxide fixation;
KW Carboxysome; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..470
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062655"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 118
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 196
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 242
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ SEQUENCE 470 AA; 52491 MW; 45B9322482745B2B CRC64;
MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA AVAAESSTGT
WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL DLFEEGSVTN VLTSLVGNVF
GFKALRALRL EDIRFPVALI KTFQGPPHGI TVERDKLNKY GRPLLGCTIK PKLGLSAKNY
GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG
TCEEMMKRAE FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE EDRSRGIFFT
QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE
ACVQARNEGR NLAREGNDVI REACRWSPEL AAACELWKEI KFEFEAMDTL
