ID   RBL2_RHOPS              Reviewed;         461 AA.
AC   Q37D32;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
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};
GN   OrderedLocusNames=RPD_1054;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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(+) = 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_01339};
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_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; CP000283; ABE38292.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q37D32; -.
DR   SMR; Q37D32; -.
DR   STRING; 316057.RPD_1054; -.
DR   KEGG; rpd:RPD_1054; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_1_5; -.
DR   BioCyc; RPAL316057:RPD_RS05355-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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   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; 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.
FT   CHAIN           1..461
FT                   /note="Ribulose bisphosphate carboxylase"
FT                   /id="PRO_0000251411"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         192
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         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         195
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   SITE            330
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT   MOD_RES         192
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
SQ   SEQUENCE   461 AA;  50500 MW;  C32F05EB00E60018 CRC64;
     MDQSNRYANL NLKESDLIAG GRHVLCAYIM KPKAGFGNFV ETAAHFAAES STGTNVEVST
     TDDFTRGVDA LVYEVDEAKE LMKIAYPIEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE
     YAKMHDFYVP PAYLRLFDGP STTIKDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFADA
     CYDFWLGGDF IKNDEPQGNQ VFAPFKDTVR AVNDAMRRAQ DATGQPKLFS FNITADDHYE
     MLARGEYILE TFGENADHVA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS
     KRGYTAFVLS KMARLQGASG IHVGTMGYGK MEGEASDRDS AFMITQDSAE GPYFKQEWLG
     MNPTTPIISG GMNALRMPGF FANLGHSNLI MTAGGGAFGH IDGGAAGARS LRQAEQCWKQ
     GADPVAFAKD HREFARAFES FPNDADKLYP NWRNMLKLAA A
//