RBL2_THIDA
ID RBL2_THIDA Reviewed; 459 AA.
AC Q60028; Q3SFL5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ribulose bisphosphate carboxylase;
DE Short=RuBisCO;
DE EC=4.1.1.39;
GN Name=cbbM; Synonyms=cbbL2; OrderedLocusNames=Tbd_2638;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], KINETIC PARAMETERS, AND FUNCTION.
RX PubMed=8550452; DOI=10.1128/jb.178.2.347-356.1996;
RA Hernandez J.M., Baker S.H., Lorbach S.C., Shively J.M., Tabita F.R.;
RT "Deduced amino acid sequence, functional expression, and unique enzymatic
RT properties of the form I and form II ribulose bisphosphate
RT carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus
RT denitrificans.";
RL J. Bacteriol. 178:347-356(1996).
RN [2]
RP SEQUENCE REVISION TO 83 AND C-TERMINUS.
RA Shively J.M.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
RN [4]
RP SUBUNIT.
RX PubMed=4623310; DOI=10.1128/jb.110.2.633-642.1972;
RA McFadden B.A., Denend A.R.;
RT "Ribulose diphosphate carboxylase from autotrophic microorganisms.";
RL J. Bacteriol. 110:633-642(1972).
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:0000269|PubMed:8550452}.
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;
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.3 uM for ribulose 1,5-bisphosphate
CC {ECO:0000269|PubMed:8550452};
CC KM=256 uM for CO(2) {ECO:0000269|PubMed:8550452};
CC KM=619 uM for O(2) {ECO:0000269|PubMed:8550452};
CC Vmax=3.3 umol/min/mg enzyme with CO(2) as substrate
CC {ECO:0000269|PubMed:8550452};
CC Vmax=0.6 umol/min/mg enzyme with O(2) as substrate
CC {ECO:0000269|PubMed:8550452};
CC Note=The CO(2)/O(2) specificity factor (tau) is 14.;
CC -!- SUBUNIT: The complex is approximately 350 kDa when isolated from either
CC T.denitrificans or R.sphaeroides, suggesting a homohexamer or
CC homooctamer structure. {ECO:0000269|PubMed:4623310}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC subfamily. {ECO:0000305}.
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DR EMBL; L37437; AAA99178.2; -; Genomic_DNA.
DR EMBL; CP000116; AAZ98591.1; -; Genomic_DNA.
DR RefSeq; WP_011313150.1; NC_007404.1.
DR AlphaFoldDB; Q60028; -.
DR SMR; Q60028; -.
DR STRING; 292415.Tbd_2638; -.
DR EnsemblBacteria; AAZ98591; AAZ98591; Tbd_2638.
DR KEGG; tbd:Tbd_2638; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_4; -.
DR OMA; NQYLHYH; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000008291; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..459
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062668"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT CONFLICT 459
FT /note="K -> S (in Ref. 1; AAA99178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50690 MW; 4E080DCFDEA4266D CRC64;
MDQSARYADL SLKEEDLIKG GRHILVAYKM KPKSGYGYLE AAAHFAAESS TGTNVEVSTT
DDFTKGVDAL VYYIDEASED MRIAYPLELF DRNVTDGRFM LVSFLTLAIG NNQGMGDIEH
AKMIDFYVPE RCIQMFDGPA TDISNLWRIL GRPVVNGGYI AGTIIKPKLG LRPEPFAKAA
YQFWLGGDFI KNDEPQGNQV FCPLKKVLPL VYDAMKRAQD DTGQAKLFSM NITADDHYEM
CARADYALEV FGPDADKLAF LVDGYVGGPG MVTTARRQYP GQYLHYHRAG HGAVTSPSAK
RGYTAFVLAK MSRLQGASGI HVGTMGYGKM EGEGDDKIIA YMIERDECQG PVYFQKWYGM
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGSYGHI DSPAAGAISL RQSYECWKQG
ADPIEFAKEH KEFARAFESF PKDADKLFPG WREKLGVHK
