RBL2_THIK1
ID RBL2_THIK1 Reviewed; 461 AA.
AC O84917; D5X1M9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=Tint_1655;
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shively J.M., Soyer F.;
RT "A form II Rubisco gene and associated genes in Thiobacillus intermedius.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP EXPRESSION IN T.INTERMEDIUS.
RX PubMed=8472910; DOI=10.1111/j.1574-6968.1993.tb06044.x;
RA Stoner M.T., Shively J.M.;
RT "Cloning and expression of the D-ribulose-1,5-bisphosphate
RT carboxylase/oxygenase form II gene from Thiobacillus intermedius in
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 107:287-292(1993).
RN [4]
RP PROBABLE EXPRESSION.
RA Shively J.M.;
RL Unpublished observations (OCT-2005).
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;
CC Evidence={ECO:0000255|HAMAP-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}.
CC -!- CAUTION: No expression of this protein has been seen during autotrophic
CC and mixotrophic growth, however the protein is probably expressed under
CC other conditions. In a related bacteria (T.neapolitanus) expression has
CC been seen when the form I enzyme has been knocked out. {ECO:0000305}.
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DR EMBL; AF012127; AAC24964.1; -; Genomic_DNA.
DR EMBL; CP002021; ADG31025.1; -; Genomic_DNA.
DR RefSeq; WP_013123277.1; NC_014153.1.
DR AlphaFoldDB; O84917; -.
DR SMR; O84917; -.
DR STRING; 75379.Tint_1655; -.
DR EnsemblBacteria; ADG31025; ADG31025; Tint_1655.
DR KEGG; tin:Tint_1655; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_4; -.
DR OMA; NQYLHYH; -.
DR BioCyc; TINT75379:TINT_RS08290-MON; -.
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; -; 1.
DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 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.
FT CHAIN 1..461
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062669"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 113
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 193
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 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT SITE 331
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT MOD_RES 193
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
SQ SEQUENCE 461 AA; 50818 MW; D470D17F356800E2 CRC64;
MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE SSTGTNVEVS
TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR FMIVSFLTLV IGNNQGMGDV
EYGKMIDFYV PERAIQMFDG PATDISNLWR ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ
AAYQFWLGGD FIKNDEPQGN QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH
EMCARADFAL EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS
SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC QGPVYFQKWY
GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG HIDSPAAGAK SLRQAYECWK
AGADPIEYAK EHKEFARAFE SFPGDADKLF PGWRDKLGVH K
