ID   RBL_PICP2               Reviewed;         470 AA.
AC   Q44176; B1XPS2;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   27-MAR-2024, entry version 146.
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   Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Picosynechococcus.
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; Evidence={ECO:0000255|HAMAP-
CC         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   KEGG; syp:SYNPCC7002_A1798; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_2_0_3; -.
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; 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   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
//