AC   MF_01339;
DC   Protein; auto
TR   HAMAP; MF_01339; -; 1; level=0
XX
Names: RuBisCO_L_type2
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ID   RBL2
DE   RecName: Full=Ribulose bisphosphate carboxylase;
DE            Short=RuBisCO;
DE            EC=4.1.1.39;
GN   Name=cbbM;
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CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site.
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.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In contrast to form I
CC       RuBisCO, the form II RuBisCO are composed solely of large subunits.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC       subfamily.
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DR   PROSITE; PS00157; RUBISCO_LARGE; 1; trigger=no
DR   Pfam; PF00016; RuBisCO_large; 1; trigger=no
DR   Pfam; PF02788; RuBisCO_large_N; 1; trigger=no
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KW   Calvin cycle
KW   Carbon dioxide fixation
KW   Lyase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
KW   Monooxygenase
KW   Oxidoreductase
case <Property:PHOTOSYN>
KW   Photosynthesis
end case
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case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0016984; F:ribulose-bisphosphate carboxylase activity
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FT   From: RBL2_RHORU (P04718)
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT   Condition: K
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT   Group: 1; Condition: K
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   SITE            329
FT                   /note="Transition state stabilizer"
FT   Condition: K
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT   Condition: N
FT   BINDING         168
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         288
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         321
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         368
FT                   /ligand="substrate"
FT   Condition: S
FT   MOD_RES         191
FT                   /note="N6-carboxylysine"
FT   Condition: K
XX
Size: 458-466;
Related: MF_01133; MF_01338;
Template: P04718;
Scope:
 Bacteria; Rhodopseudomonas
 Bacteria; Rhodobacterales
 Bacteria; Rhodospirillales
 Bacteria; Comamonadaceae
 Bacteria; Thiomonas
 Bacteria; Hydrogenophilales
 Bacteria; Rhodocyclaceae
 Bacteria; Halothiobacillus
 Bacteria; Hydrogenovibrio
 Bacteria; Thiomicrospira
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.20 2022/11/19
//