RBL2_POLNA
ID RBL2_POLNA Reviewed; 459 AA.
AC A1VNQ9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Pnap_1978;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
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}.
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DR EMBL; CP000529; ABM37287.1; -; Genomic_DNA.
DR RefSeq; WP_011801368.1; NC_008781.1.
DR AlphaFoldDB; A1VNQ9; -.
DR SMR; A1VNQ9; -.
DR STRING; 365044.Pnap_1978; -.
DR PRIDE; A1VNQ9; -.
DR EnsemblBacteria; ABM37287; ABM37287; Pnap_1978.
DR KEGG; pna:Pnap_1978; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_4; -.
DR OMA; NQYLHYH; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000000644; 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; -; 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; Reference proteome.
FT CHAIN 1..459
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_1000067649"
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; 50571 MW; 6FEEDE1CB0783D9D CRC64;
MDQSNRYADL SLKEEDLIAG GRHILVAYKM KPKAGHGYLE AAAHFAAESS TGTNVEVSTT
DEFTKGVDAL VYLIDEATEE MRIAFPMDLF DRNILDGRMM IVSFLTLVIG NNQGMGDIQH
AKIYDFFMPP RAIQLFDGPS KDISDMWRIL GRPVKDGGYI AGTIIKPKLG LRPEPFAQAA
YQFWLGGDFI KNDEPQGNQT FAPMNKVMPL VHDAMKRAMD ETGEAKLFSA NITADDHYEM
LARGDYILRT FGPDADKVAF LVDGYVGGPG MITTARRAFP NQYLHYHRAG HGAVTSPSAK
RGYDAYVLAK MSRLQGASGI HVGTMGYGKM EGTHDDRAIA YIIERDSYTG PAYHQEWYGM
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGAYGHI DSPAAGATSL RQAYECWKAK
ADPIEWAKEH PEFARAFASF PGDADMLFPG WRDKLASHR
