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   27-MAR-2024, entry version 153.
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; Cyanobacteriota; Cyanophyceae; 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; 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 (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   PDB; 7XSD; EM; 3.30 A; A/B/C/D/E/F/G/H=1-476.
DR   PDBsum; 6KKM; -.
DR   PDBsum; 6LRR; -.
DR   PDBsum; 6LRS; -.
DR   PDBsum; 6Z1F; -.
DR   PDBsum; 6Z1G; -.
DR   PDBsum; 7XSD; -.
DR   AlphaFoldDB; P00879; -.
DR   EMDB; EMD-0959; -.
DR   EMDB; EMD-0960; -.
DR   EMDB; EMD-11028; -.
DR   EMDB; EMD-11029; -.
DR   SMR; P00879; -.
DR   STRING; 103690.gene:10493537; -.
DR   KEGG; ana:alr1524; -.
DR   eggNOG; COG1850; Bacteria.
DR   OrthoDB; 9770811at2; -.
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; 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; 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;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="F -> S (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="S -> Y (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="G -> V (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="T -> N (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="V -> L (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399
FT                   /note="S -> F (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/AAA22027/AAA22028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="P -> R (in Ref. 1; AAA22041 and 2;
FT                   AAA22024/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   TURN            204..206
FT                   /evidence="ECO:0007829|PDB:7XSD"
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
//