RBL_PYRFU
ID RBL_PYRFU Reviewed; 420 AA.
AC Q8U1P9;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01133};
DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01133};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01133};
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01133}; OrderedLocusNames=PF1156;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to
CC ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-
CC phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation
CC pathway, together with AMP phosphorylase and R15P isomerase.
CC {ECO:0000255|HAMAP-Rule:MF_01133}.
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_01133};
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_01133};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01133};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01133};
CC -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO, the
CC form III RuBisCO is composed solely of large subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01133}.
CC -!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO are
CC all anaerobic, it is most likely that only the carboxylase activity of
CC RuBisCO, and not the competitive oxygenase activity (by which RuBP
CC reacts with O(2) to form one molecule of 3-phosphoglycerate and one
CC molecule of 2-phosphoglycolate), is biologically relevant in these
CC strains. {ECO:0000255|HAMAP-Rule:MF_01133}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01133}.
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DR EMBL; AE009950; AAL81280.1; -; Genomic_DNA.
DR RefSeq; WP_011012296.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U1P9; -.
DR SMR; Q8U1P9; -.
DR STRING; 186497.PF1156; -.
DR EnsemblBacteria; AAL81280; AAL81280; PF1156.
DR GeneID; 41712965; -.
DR KEGG; pfu:PF1156; -.
DR PATRIC; fig|186497.12.peg.1217; -.
DR eggNOG; arCOG04443; Archaea.
DR HOGENOM; CLU_031450_3_1_2; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 9533at2157; -.
DR PhylomeDB; Q8U1P9; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR CDD; cd08213; RuBisCO_large_III; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01133; RuBisCO_L_type3; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR017712; RuBisCO_III.
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 PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 2.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR TIGRFAMs; TIGR03326; rubisco_III; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..420
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062676"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 343..345
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT BINDING 365..368
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
FT MOD_RES 181
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01133"
SQ SEQUENCE 420 AA; 47348 MW; 0271D055DCFF3DC4 CRC64;
MKVEWYLDFV DLDYTPGRDE LIVEYYFEPN GVSPEEAAGR IASESSIGTW TTLWKMPEMA
KRSMAKVFYL EKSGEGYIAK IAYPLTLFEE GSIVQLLSAI AGNIFGMKAL KNLRLLDFHP
PYEYLRHFKG PQYGVKGIRE FMGVKERPLT ATVPKPKMGW SVDEYAEIAY ELWSGGIDLL
KDDENFTSFP FNRFEERVKK LYRIRDIVEA ETEERKEYLI NITGSVDVME KRAELVANEG
GQYVMIDIIV TGWSALQYMR EVTEDLGLAI HAHRAMHAAF TRNPKHGITM YAIAKLARMI
GVDQIHTGTA VGKMAGDYEE VKRINDFLLS KWEHIREVFP VASGGLHPGL MPELIRLFGK
DLVIQAGGGV MGHPDGPRAG AKALRDAIDA ALEGVDLEEK AKSSPELKKA LDKWGYLKPK
