RBL_THEVB
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 03-AUG-2022, entry version 120.
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}; OrderedLocusNames=tll1506;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC 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;
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 (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; 197221.22295231; -.
DR PRIDE; Q8DIS5; -.
DR EnsemblBacteria; BAC09058; BAC09058; BAC09058.
DR KEGG; tel:tll1506; -.
DR PATRIC; fig|197221.4.peg.1580; -.
DR eggNOG; COG1850; Bacteria.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
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; -; 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; 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
