ID I3RER9_9EURY Unreviewed; 420 AA.
AC I3RER9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|HAMAP-Rule:MF_01133};
DE Short=RuBisCO {ECO:0000256|HAMAP-Rule:MF_01133};
DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01133};
GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01133};
GN ORFNames=Py04_1155 {ECO:0000313|EMBL:AFK22729.1};
OS Pyrococcus sp. ST04.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=1183377 {ECO:0000313|EMBL:AFK22729.1, ECO:0000313|Proteomes:UP000006467};
RN [1] {ECO:0000313|EMBL:AFK22729.1, ECO:0000313|Proteomes:UP000006467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST04 {ECO:0000313|EMBL:AFK22729.1,
RC ECO:0000313|Proteomes:UP000006467};
RX PubMed=22843576; DOI=10.1128/JB.00824-12;
RA Jung J.H., Lee J.H., Holden J.F., Seo D.H., Shin H., Kim H.Y., Kim W.,
RA Ryu S., Park C.S.;
RT "Complete Genome Sequence of the Hyperthermophilic Archaeon Pyrococcus sp.
RT Strain ST04, Isolated from a Deep-Sea Hydrothermal Sulfide Chimney on the
RT Juan de Fuca Ridge.";
RL J. Bacteriol. 194:4434-4435(2012).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01133};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01133};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01133}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01133}.
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DR EMBL; CP003534; AFK22729.1; -; Genomic_DNA.
DR RefSeq; WP_014734253.1; NC_017946.1.
DR AlphaFoldDB; I3RER9; -.
DR STRING; 1183377.Py04_1155; -.
DR GeneID; 13022403; -.
DR KEGG; pys:Py04_1155; -.
DR eggNOG; arCOG04443; Archaea.
DR HOGENOM; CLU_031450_3_1_2; -.
DR OrthoDB; 52787at2157; -.
DR Proteomes; UP000006467; 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; 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_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 NCBIfam; TIGR03326; rubisco_III; 1.
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; SFLDG01052; RuBisCO; 1.
DR SFLD; SFLDS00014; RuBisCO; 2.
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.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01133};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01133};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01133};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01133}.
FT DOMAIN 8..124
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 134..414
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01133"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 343..345
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 365..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT MOD_RES 181
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ SEQUENCE 420 AA; 47262 MW; 85885F42443D3B99 CRC64;
MKVEWYLDFV DLEYSPGRDE LIVEYYFEPN GVSPEEAAGR IASESSIGTW TTLWKMPEMA
KRSMAKVFYL EKKGDGYIAK IAYPLTLFEE GSLVQLFSAI AGNIFGMKAI KNLRLLDFHP
PYEYLRHFRG PQYGVNGIRE FMGVHDRPLT ATVPKPKMGW SVEEYAEIAY ELWSGGIDLL
KDDENFTSFP FNRFEERVRK LYRVRDRVEA ETGETKEYLI NITGPVNVME KRAEMVANEG
GQYVMIDIVV AGWSALQYMR EVTEDLGLAI HAHRAMHAAF TRNPKHGITM LALAKAARMI
GVDQIHTGTA VGKMAGDYEE IKRINDFLLS RWEHIRPVFP VASGGLHPGL MPELIRLFGK
DLVIQAGGGV MGHPDGPKAG AKALRDAIEA AVDGIDLEEK AKSSPELRKA LDKWGYLKPK
//
