RBL_NOSS1
ID RBL_NOSS1 Reviewed; 476 AA.
AC P00879; Q60124;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 148.
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:32451445};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=rbc, rbcA, rbcL {ECO:0000255|HAMAP-Rule:MF_01338,
GN ECO:0000303|PubMed:6091125}; OrderedLocusNames=alr1524;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=16593300; DOI=10.1073/pnas.80.7.1835;
RA Curtis S.E., Haselkorn R.;
RT "Isolation and sequence of the gene for the large subunit of ribulose-1,5-
RT bisphosphate carboxylase from the cyanobacterium Anabaena 7120.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:1835-1839(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=6091125; DOI=10.1073/pnas.81.19.5961;
RA Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R.;
RT "Cotranscription of genes encoding the small and large subunits of
RT ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena
RT 7120.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [4]
RP PROTEIN SEQUENCE OF 16-22, AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24907906; DOI=10.1007/s11120-014-0018-4;
RA de Araujo C., Arefeen D., Tadesse Y., Long B.M., Price G.D., Rowlett R.S.,
RA Kimber M.S., Espie G.S.;
RT "Identification and characterization of a carboxysomal gamma-carbonic
RT anhydrase from the cyanobacterium Nostoc sp. PCC 7120.";
RL Photosyn. Res. 121:135-150(2014).
RN [6] {ECO:0007744|PDB:6KKM, ECO:0007744|PDB:6LRR, ECO:0007744|PDB:6LRS}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH RAF1, STRUCTURE BY
RP ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH RBCS AND RAF1,
RP FUNCTION, RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, AND DISULFIDE BOND.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=32451445; DOI=10.1038/s41477-020-0665-8;
RA Xia L.Y., Jiang Y.L., Kong W.W., Sun H., Li W.F., Chen Y., Zhou C.Z.;
RT "Molecular basis for the assembly of RuBisCO assisted by the chaperone
RT Raf1.";
RL Nat. Plants 6:708-717(2020).
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:32451445};
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) (PubMed:32451445). Forms complexes of many
CC stoichiometries with Raf1 with and without RbcS (PubMed:32451445).
CC RuBisCO interacts with the C-terminus of CcmM (By similarity).
CC {ECO:0000250|UniProtKB:Q31NB3, ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|PubMed:32451445}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|PubMed:24907906}. Note=This cyanobacterium makes beta-type
CC carboxysomes (PubMed:24907906). In the carboxysome RuBisCO is organized
CC into a paracrystalline array (By similarity).
CC {ECO:0000250|UniProtKB:Q31NB3, ECO:0000269|PubMed:24907906}.
CC -!- INDUCTION: Part of the rbcL-rbcS operon, transcribed in light and
CC constitutively during growth on fructose. {ECO:0000269|PubMed:6091125}.
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 -!- MASS SPECTROMETRY: Mass=53411; Method=MALDI;
CC Evidence={ECO:0000269|Ref.4};
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 dimeric Raf1 binds to RbcL(2) leading to an RbcL8-Raf1(8) complex. RbcS
CC displaces Raf1, resulting in holoenzyme formation.
CC {ECO:0000269|PubMed:32451445}.
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; J01540; AAA22041.1; -; Genomic_DNA.
DR EMBL; L02520; AAA22024.1; -; Genomic_DNA.
DR EMBL; L02521; AAA22027.1; -; Genomic_DNA.
DR EMBL; L02522; AAA22028.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB77890.1; -; Genomic_DNA.
DR PIR; A01099; RKAIL7.
DR PIR; AF1996; AF1996.
DR RefSeq; WP_010995693.1; NZ_RSCN01000022.1.
DR PDB; 6KKM; X-ray; 3.00 A; A/B/C/D=1-476.
DR PDB; 6LRR; EM; 3.37 A; A/B/C/D/E/F/G/H=1-476.
DR PDB; 6LRS; EM; 3.37 A; A/B/C/D/E/F/G/H=1-476.
DR PDB; 6Z1F; EM; 2.86 A; A/B/C/D/E/F/G/H=1-476.
DR PDB; 6Z1G; EM; 8.20 A; B/C=1-476.
DR PDBsum; 6KKM; -.
DR PDBsum; 6LRR; -.
DR PDBsum; 6LRS; -.
DR PDBsum; 6Z1F; -.
DR PDBsum; 6Z1G; -.
DR AlphaFoldDB; P00879; -.
DR SMR; P00879; -.
DR STRING; 103690.17135344; -.
DR EnsemblBacteria; BAB77890; BAB77890; BAB77890.
DR KEGG; ana:alr1524; -.
DR eggNOG; COG1850; Bacteria.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000002483; 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 3D-structure; Bacterial microcompartment; Calvin cycle;
KW Carbon dioxide fixation; Carboxysome; Direct protein sequencing;
KW Disulfide bond; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis; Reference proteome.
FT CHAIN 1..476
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062619"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 295
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 124
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 202
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 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 335
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 202
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 248
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:32451445, ECO:0007744|PDB:6KKM,
FT ECO:0007744|PDB:6LRR"
FT CONFLICT 91
FT /note="V -> G (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="F -> S (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> Y (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="G -> V (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="T -> N (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="V -> L (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="S -> F (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="P -> R (in Ref. 1; AAA22041 and 2; AAA22024/
FT AAA22027/AAA22028)"
FT /evidence="ECO:0000305"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6LRR"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:6Z1F"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6KKM"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6KKM"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6KKM"
FT HELIX 215..233
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6Z1F"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 414..434
FT /evidence="ECO:0007829|PDB:6Z1F"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:6Z1F"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:6Z1F"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6Z1F"
SQ SEQUENCE 476 AA; 53045 MW; ABEDB246FA2E6A01 CRC64;
MSYAQTKTQT KSGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP FEEAAAAVAA
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA YIAYPLDLFE EGSITNVLTS
IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG
LSAKNYGRAV YECLRGGLDF TKDDENINSA PFQRWRDRFL FVADAITKAQ AETGEIKGHY
LNVTAPTCEE MLKRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGV LLHIHRAMHA
VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL RENYVEQDKS
RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH PWGNAPGATA
NRVALEACVQ ARNEGRNLAR EGNDVIREAA KWSPELAVAC ELWKEIKFEF EAMDTV
