ID   G0HNE1_THES4            Unreviewed;       444 AA.
AC   G0HNE1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   ECO:0000313|EMBL:AEK73792.1};
GN   OrderedLocusNames=GQS_09490 {ECO:0000313|EMBL:AEK73792.1};
OS   Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73792.1, ECO:0000313|Proteomes:UP000000874};
RN   [1] {ECO:0000313|EMBL:AEK73792.1, ECO:0000313|Proteomes:UP000000874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX   PubMed=21914870; DOI=10.1128/JB.05851-11;
RA   Wang X., Gao Z., Xu X., Ruan L.;
RT   "Complete genome sequence of Thermococcus sp. strain 4557, a
RT   hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT   area.";
RL   J. Bacteriol. 193:5544-5545(2011).
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; Evidence={ECO:0000256|HAMAP-
CC         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; CP002920; AEK73792.1; -; Genomic_DNA.
DR   RefSeq; WP_014013474.1; NC_015865.1.
DR   AlphaFoldDB; G0HNE1; -.
DR   STRING; 1042877.GQS_09490; -.
DR   GeneID; 11016580; -.
DR   KEGG; the:GQS_09490; -.
DR   PATRIC; fig|1042877.9.peg.1851; -.
DR   eggNOG; arCOG04443; Archaea.
DR   HOGENOM; CLU_031450_3_1_2; -.
DR   OrthoDB; 52787at2157; -.
DR   Proteomes; UP000000874; 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, ECO:0000313|EMBL:AEK73792.1};
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          12..132
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          142..438
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         189
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         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         367..369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   BINDING         389..392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   SITE            322
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT   MOD_RES         189
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ   SEQUENCE   444 AA;  50281 MW;  7636B3F260130FC7 CRC64;
     MVEKFDEIYD YYVDKAYEPN KKRDIIAVFR ITPAKGYTIE AAAGAVAAES STGTWTTLYE
     WYEKERWADL SAKAYDFHDM GDGSWIVKIA YPSHAFEDGN MPGFLASIAG NIFGMKRVEW
     LRLEDIYLPE RFLRNYPGPN FGIEGVRKKL EIYDRPLYGV VPKPKVGYSP EELYKLANDL
     FLGGADYIKD DENLTSPWYN RFEERVKIVT KAMERAENET GEKKTWFANI TAPILEMEER
     LEILADYGVP HAMIDVVVLG WGVLDYIREL ADDYGIALHA HRAMHTAFAR NPYHGISMFV
     LAKLYRLIGV DQLHIGTAGA GKMEGEKWEV IQYKRIITED HYVPDENDVF HLEQKFYHIK
     PVFPTSSGGL HPGNIQPVID ALGKDIVLQL GGGTMGHPDG PKAGAMAVRQ ALDAIMQGIP
     LDEYAKSHRE LARALEKWGH VTPV
//