AC   MF_01133;
DC   Protein; auto
TR   HAMAP; MF_01133; -; 1; level=0
XX
Names: RuBisCO_L_type3
XX
ID   RBL
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=rbcL;
XX
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   -!- 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;
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;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
CC   -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO, the
CC       form III RuBisCO is composed solely of large subunits.
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.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III
CC       subfamily.
XX
DR   Pfam; PF00016; RuBisCO_large; 1; trigger=no
DR   Pfam; PF02788; RuBisCO_large_N; 1; trigger=no
DR   NCBIfam; TIGR03326; rubisco_III; 1; trigger=no
XX
KW   Carbon dioxide fixation
KW   Lyase
KW   Oxidoreductase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0016984; F:ribulose-bisphosphate carboxylase activity
GO   GO:0006196; P:AMP catabolic process
XX
FT   From: RBL_THEKO (O93627)
FT   BINDING         367..369
FT                   /ligand="substrate"
FT   Condition: S-x-G
FT   BINDING         389..392
FT                   /ligand="substrate"
FT   Condition: Q-x-G-G
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT   Condition: K
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT   Group: 1; Condition: K
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         165
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         282
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         314
FT                   /ligand="substrate"
FT   Condition: H
FT   SITE            322
FT                   /note="Transition state stabilizer"
FT   Condition: K
FT   MOD_RES         189
FT                   /note="N6-carboxylysine"
FT   Condition: K
XX
Size: 410-450;
Related: MF_01338; MF_01339;
Template: O93627; Q58632; O28635; Q8THG2;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.35 2023/06/01
//