RBL_SYNP2
ID RBL_SYNP2 Reviewed; 470 AA.
AC Q44176; B1XPS2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 141.
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 OrderedLocusNames=SYNPCC7002_A1798;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Akiyama H., Kanai S., Hirano M., Sugimoto M., Kiyohara M.;
RT "Cloning and characterization of RubisCO large subunit and small subunit
RT from Synechococcus sp. PCC7002.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=20075914; DOI=10.1038/nature08651;
RA Liu C., Young A.L., Starling-Windhof A., Bracher A., Saschenbrecker S.,
RA Rao B.V., Rao K.V., Berninghausen O., Mielke T., Hartl F.U., Beckmann R.,
RA Hayer-Hartl M.;
RT "Coupled chaperone action in folding and assembly of hexadecameric
RT Rubisco.";
RL Nature 463:197-202(2010).
RN [4]
RP RUBISCO FOLDING AND ASSEMBLY, INTERACTION WITH RAF1, AND SUBUNIT.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=26237510; DOI=10.1038/nsmb.3062;
RA Hauser T., Bhat J.Y., Milicic G., Wendler P., Hartl F.U., Bracher A.,
RA Hayer-Hartl M.;
RT "Structure and mechanism of the Rubisco-assembly chaperone Raf1.";
RL Nat. Struct. Mol. Biol. 22:720-728(2015).
RN [5] {ECO:0007744|PDB:2PEM}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 459-465 IN COMPLEX WITH RBCX2,
RP RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, AND MUTAGENESIS OF 460-ILE--LEU-470;
RP PHE-462 AND PHE-464.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=17574029; DOI=10.1016/j.cell.2007.04.025;
RA Saschenbrecker S., Bracher A., Rao K.V., Rao B.V., Hartl F.U.,
RA Hayer-Hartl M.;
RT "Structure and function of RbcX, an assembly chaperone for hexadecameric
RT Rubisco.";
RL Cell 129:1189-1200(2007).
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 (Probable). {ECO:0000305|PubMed:17574029}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338}.
CC Note=In the carboxysome RuBisCO is organized into a paracrystalline
CC array (By similarity). This cyanobacterium makes beta-type carboxysomes
CC (Probable). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000305}.
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: RuBisCO folding and assembly commences when the nascent
CC large subunit folds with the help of the chaperonin GroEL-GroES.
CC Requires homodimeric RuBisCO chaperone RbcX2 to assemble into RbcL8
CC octamers, making RbcL8-(RbcX2)8. The exposed C-terminus of RbcL binds
CC in a cleft in RbcX2 (PubMed:17574029, PubMed:20075914). RbcX2 is
CC displaced by RbcS; as RbcX2 is removed RbcS mediates the ordering of an
CC internal RbcL loop (Thr-63-Leu-69) in a catalytically active
CC conformation (By similarity). Interacts with accumulation factor Raf1;
CC dimeric Raf1 acts after chaperonin GroEL-GroES, binding to RbcL(2)
CC leading to an RbcL8-Raf1(8) complex. RbcS displaces Raf1, resulting in
CC holoenzyme formation (PubMed:26237510). {ECO:0000250|UniProtKB:P00880,
CC ECO:0000269|PubMed:17574029, ECO:0000269|PubMed:20075914,
CC ECO:0000269|PubMed:26237510}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACA99786.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D13971; BAA03076.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA99786.1; ALT_INIT; Genomic_DNA.
DR PDB; 2PEM; X-ray; 2.95 A; R=459-465.
DR PDBsum; 2PEM; -.
DR AlphaFoldDB; Q44176; -.
DR SMR; Q44176; -.
DR STRING; 32049.SYNPCC7002_A1798; -.
DR EnsemblBacteria; ACA99786; ACA99786; SYNPCC7002_A1798.
DR KEGG; syp:SYNPCC7002_A1798; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_3; -.
DR OMA; IHGHPDG; -.
DR Proteomes; UP000001688; 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 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 3D-structure; Bacterial microcompartment; Calvin cycle;
KW Carbon dioxide fixation; Carboxysome; Disulfide bond; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..470
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062650"
FT MOTIF 459..465
FT /note="Interacts with RbcX2"
FT /evidence="ECO:0000269|PubMed:17574029"
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"
FT MUTAGEN 460..470
FT /note="Missing: Does not assemble into RbcL8, does not
FT interact with RbcX2."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 462
FT /note="F->A: Does not assemble into RbcL8, does not
FT interact with RbcX2."
FT /evidence="ECO:0000269|PubMed:17574029"
FT MUTAGEN 464
FT /note="F->A: Decreased assembly of RbcL8, decreased
FT interaction with RbcX2."
FT /evidence="ECO:0000269|PubMed:17574029"
SQ SEQUENCE 470 AA; 52159 MW; 7D43456FD17D9775 CRC64;
MQTKSAGFNA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPPEECAA AVAAESSTGT
WTTVWTDGLT DLDRYKGRCY NVEPVPGEDN QYFCFVAYPL DLFEEGSVTN VLTSLVGNVF
GFKALRALRL EDIRFPVALI KTYQGPPHGI TVERDLLNKY GRPLLGCTIK PKLGLSAKNY
GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKSQAETNEV KGHYLNVTAG
TCEEMLKRAE FAKEIGTPII MHDFLTGGFT ANTTLAKWCR DNGVLLHIHR AMHAVIDRQK
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGDRAATLGF VDLMREDYVE EDRSRGVFFT
QDYASLPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE
ACVQARNEGR SLAREGNDVL REAGKWSPEL AAALDLWKEI KFEFDTVDTL
