ID   RBL2_CERS4              Reviewed;         459 AA.
AC   Q3IX55;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   02-SEP-2026, entry version 104.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339};
DE            Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339};
GN   Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339}; Synonyms=rbpL;
GN   OrderedLocusNames=RHOS4_33110; ORFNames=RSP_3271;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. Both reactions occur simultaneously and in competition at
CC       the same active site. {ECO:0000255|HAMAP-Rule:MF_01339}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5-
CC         bisphosphate + CO2 + 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_01339};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)-
CC         3-phosphoglycerate + 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_01339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01339};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01339};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01339}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In contrast to form I
CC       RuBisCO, the form II RuBisCO are composed solely of large subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01339}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01339}.
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DR   EMBL; CP000144; ABA80879.1; -; Genomic_DNA.
DR   RefSeq; WP_011339170.1; NC_007494.2.
DR   AlphaFoldDB; Q3IX55; -.
DR   SMR; Q3IX55; -.
DR   STRING; 272943.RSP_3271; -.
DR   EnsemblBacteria; ABA80879; ABA80879; RSP_3271.
DR   GeneID; 3721872; -.
DR   GeneID; 48981336; -.
DR   KEGG; rsp:RSP_3271; -.
DR   PATRIC; fig|272943.9.peg.3698; -.
DR   eggNOG; COG1850; Bacteria.
DR   OrthoDB; 9764279at2; -.
DR   PhylomeDB; Q3IX55; -.
DR   Proteomes; UP000002703; Chromosome 2.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   CDD; cd08211; RuBisCO_large_II; 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_01339; RuBisCO_L_type2; 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; IPR020871; RuBisCO_lsuII.
DR   NCBIfam; NF010002; PRK13475.1; 1.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF17; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN           1..459
FT                   /note="Ribulose bisphosphate carboxylase"
FT                   /id="PRO_0000251413"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   SITE            329
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   MOD_RES         191
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
SQ   SEQUENCE   459 AA;  50601 MW;  1B6DC87E1CC1DDF1 CRC64;
     MDQSNRYARL DLQEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS TGTNVEVSTT
     DDFTRGVDAL VYEIDPEKEI MKIAYPVELF DRNIIDGRAM LCSFLTLTIG NNQGMGDVEY
     AKMHDFYVPP CYLRLFDGPS MNIADMWRVL GRDVRNGGMV VGTIIKPKLG LRPKPFADAC
     HEFWLGGDFI KNDEPQGNQT FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM
     VARGEYILET FGENADHVAF LVDGYVTGPA AITTARRQFP RQFLHYHRAG HGAVTSPQSM
     RGYTAFVLSK MARLQGASGI HTGTMGYGKM EGEAADKIMA YMLTDEAAEG PFYRQDWLGL
     KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL DGGTAGAKSL RQSHEAWMAG
     VDLVTYAREH RELARAFESF PADADKFYPG WRDRLHRAA
//