ID   RBL_THEVB               Reviewed;         475 AA.
AC   Q8DIS5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
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, ECO:0000269|PubMed:25041569};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=tll1506;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Thermosynechococcaceae; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [2]
RP   RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=19081849;
RA   Tarnawski M., Gubernator B., Kolesinski P., Szczepaniak A.;
RT   "Heterologous expression and initial characterization of recombinant RbcX
RT   protein from Thermosynechococcus elongatus BP-1 and the role of RbcX in
RT   RuBisCO assembly.";
RL   Acta Biochim. Pol. 55:777-785(2008).
RN   [3]
RP   FUNCTION, RUBISCO FOLDING AND ASSEMBLY, INTERACTION WITH RAF1, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=25041569; DOI=10.1111/febs.12928;
RA   Kolesinski P., Belusiak I., Czarnocki-Cieciura M., Szczepaniak A.;
RT   "Rubisco Accumulation Factor 1 from Thermosynechococcus elongatus
RT   participates in the final stages of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase assembly in Escherichia coli cells and in vitro.";
RL   FEBS J. 281:3920-3932(2014).
RN   [4] {ECO:0007744|PDB:2YBV, ECO:0007744|PDB:3ZXW}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SUBUNIT, AND DISULFIDE BOND.
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RA   Terlecka B., Wilhelmi V., Bialek W., Gubernator B., Szczepaniak A.,
RA   Hofmann E.;
RT   "Structure of Ribulose-1,5-Bisphosphate Carboxylase Oxygenase from
RT   Thermosynechococcus Elongatus.";
RL   Submitted (MAR-2011) to the PDB data bank.
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, ECO:0000269|PubMed:25041569};
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 (PubMed:25041569, Ref.4). The disulfide link is formed
CC       within the large subunit homodimers (Ref.4). Interacts with assembly
CC       factor Raf1 which helps form the holoenzyme, most interaction (and
CC       folding) occurs in the cytoplasm (PubMed:25041569).
CC       {ECO:0000269|PubMed:25041569, ECO:0000269|Ref.4}.
CC   -!- INTERACTION:
CC       Q8DIS5; Q8DI26: raf1; NbExp=2; IntAct=EBI-9639313, EBI-9639332;
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338,
CC       ECO:0000269|PubMed:25041569}. Cytoplasm {ECO:0000269|PubMed:25041569}.
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 chaperonin GroEL-GroES. Both RbcX
CC       and Raf1 help folded RbcL release from the chaperonin and dimerize
CC       (Probable). Dimeric Raf1 binds to RbcL(2) leading to an RbcL8-Raf1(8)
CC       complex. RbcS displaces Raf1, resulting in holoenzyme formation (By
CC       similarity). {ECO:0000250|UniProtKB:P00879,
CC       ECO:0000305|PubMed:19081849, ECO:0000305|PubMed:25041569}.
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, ECO:0000269|PubMed:25041569,
CC       ECO:0000269|Ref.4}.
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; BA000039; BAC09058.1; -; Genomic_DNA.
DR   RefSeq; NP_682296.1; NC_004113.1.
DR   RefSeq; WP_011057346.1; NC_004113.1.
DR   PDB; 2YBV; X-ray; 2.30 A; A/C/E/G/I/K/M/O=1-475.
DR   PDB; 3ZXW; X-ray; 2.10 A; A/C/E/G=1-475.
DR   PDB; 6EKC; X-ray; 2.63 A; A1/A2/A3/A4/A5/A6/A7/A8/C1/C2/C3/C4/C5/C6/C7/C8/E1/E2/E3/E4/E5/E6/E7/E8/G1/G2/G3/G4/G5/G6=1-475.
DR   PDBsum; 2YBV; -.
DR   PDBsum; 3ZXW; -.
DR   PDBsum; 6EKC; -.
DR   AlphaFoldDB; Q8DIS5; -.
DR   SMR; Q8DIS5; -.
DR   IntAct; Q8DIS5; 1.
DR   MINT; Q8DIS5; -.
DR   STRING; 197221.gene:10748106; -.
DR   EnsemblBacteria; BAC09058; BAC09058; BAC09058.
DR   KEGG; tel:tll1506; -.
DR   PATRIC; fig|197221.4.peg.1580; -.
DR   eggNOG; COG1850; Bacteria.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062649"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         201
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         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            334
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         201
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   DISULFID        247
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT                   ECO:0000269|Ref.4, ECO:0007744|PDB:2YBV,
FT                   ECO:0007744|PDB:3ZXW"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           182..194
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           214..232
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           247..259
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           274..287
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           298..302
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           311..321
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          324..327
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           339..350
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          375..381
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           384..386
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           387..394
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   STRAND          396..401
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           404..407
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           413..431
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   TURN            437..439
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           441..451
FT                   /evidence="ECO:0007829|PDB:3ZXW"
FT   HELIX           453..462
FT                   /evidence="ECO:0007829|PDB:3ZXW"
SQ   SEQUENCE   475 AA;  53025 MW;  B4A97CD4D6A3EB91 CRC64;
     MAYTQSKSQK VGYQAGVKDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPF EEAAAAVAAE
     SSTGTWTTVW TDLLTDLDRY KGCCYDIEPL PGEDNQFIAY IAYPLDLFEE GSVTNMLTSI
     VGNVFGFKAL KALRLEDLRI PVAYLKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEIKGHYL
     NVTAPTCEEM LKRAEFAKEL EMPIIMHDFL TAGFTANTTL SKWCRDNGML LHIHRAMHAV
     MDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA VTLGFVDLLR ENYIEQDRSR
     GIYFTQDWAS MPGVMAVASG GIHVWHMPAL VDIFGDDAVL QFGGGTLGHP WGNAPGATAN
     RVALEACIQA RNEGRDLMRE GGDIIREAAR WSPELAAACE LWKEIKFEFE AQDTI
//