ID A0A2I8VFH6_9EURY Unreviewed; 414 AA.
AC A0A2I8VFH6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 18-JUN-2025, entry version 24.
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:AUV80692.1};
GN ORFNames=C2R22_02660 {ECO:0000313|EMBL:AUV80692.1};
OS Salinigranum rubrum.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloferacaceae; Salinigranum.
OX NCBI_TaxID=755307 {ECO:0000313|EMBL:AUV80692.1, ECO:0000313|Proteomes:UP000236584};
RN [1] {ECO:0000313|EMBL:AUV80692.1, ECO:0000313|Proteomes:UP000236584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GX10 {ECO:0000313|EMBL:AUV80692.1,
RC ECO:0000313|Proteomes:UP000236584};
RA Han S.;
RT "Complete genome sequence of Salinigranum rubrum GX10T, an extremely
RT halophilic archaeon isolated from a marine solar saltern.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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(+) = D-ribulose 1,5-
CC bisphosphate + CO2 + 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 = 2-phosphoglycolate + (2R)-
CC 3-phosphoglycerate + 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; CP026309; AUV80692.1; -; Genomic_DNA.
DR RefSeq; WP_103424300.1; NZ_CP026309.1.
DR AlphaFoldDB; A0A2I8VFH6; -.
DR GeneID; 35590955; -.
DR KEGG; srub:C2R22_02660; -.
DR OrthoDB; 52787at2157; -.
DR Proteomes; UP000236584; 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 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; NF003252; PRK04208.1; 1.
DR NCBIfam; TIGR03326; rubisco_III; 1.
DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF17; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
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|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_01133}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000236584}.
FT DOMAIN 8..117
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 137..408
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 176
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 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 337..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT BINDING 359..362
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT SITE 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
FT MOD_RES 176
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133"
SQ SEQUENCE 414 AA; 44604 MW; CBA72AF90B58F858 CRC64;
MTGITYEDFL DLSYEPSDAD LVCEFHVEPA ADMEIEAAAS RVASESSNGT WAELQVEECV
DLSATACDID GSRVTVAYPD ALFEPGNMPQ VLSCIAGNIM GMKAVERIRL LDCRWPEGLA
TSFPGPQFGS RVRDEIFDAG DRPILATVPK PKVGLPTKEH VRVGREAWLG GIDLLKDDEN
LTDQSFNPYE DRLTESLAAR DEAEEATGES KSYLVNVTGP THDMLERVDR AAEEGCEYVM
VDVVTTGWGA VQTVRDACES HGVAIHAHRA MHAAFDRIET HGVSMRVIAQ LARLCGVDQI
HTGTADLGKL ANEDTVGINE WLYSDLYGLR DVLPVASGGL HPGLVPELVS RVGTNVCIQA
GGGIHGHPGG THDGAKALRQ ATDATVAGVS LEEYATDYPE LAVAMEKWGT ETPR
//
