AC   MF_02230;
DC   Protein; auto
TR   HAMAP; MF_02230; -; 1; level=0
XX
Names: R15P_isomerase
XX
ID   R15PI
DE   RecName: Full=Ribose 1,5-bisphosphate isomerase;
DE            Short=R15P isomerase;
DE            Short=R15Pi;
DE            EC=5.3.1.29;
DE   AltName: Full=Ribulose 1,5-bisphosphate synthase;
DE            Short=RuBP synthase;
XX
case <OC:Halobacteria>
CC   -!- FUNCTION: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P)
CC       to ribulose 1,5-bisphosphate (RuBP).
else
CC   -!- FUNCTION: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P)
CC       to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate
CC       for RubisCO. Functions in an archaeal AMP degradation pathway, together
CC       with AMP phosphorylase and RubisCO.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate;
CC         Xref=Rhea:RHEA:32243, ChEBI:CHEBI:57870, ChEBI:CHEBI:68688;
CC         EC=5.3.1.29;
CC   -!- MISCELLANEOUS: Reaction proceeds via a cis-phosphoenolate intermediate.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       R15P isomerase subfamily.
XX
DR   Pfam; PF01008; IF-2B; 1; trigger=no
DR   NCBIfam; TIGR00524; eIF-2B_rel; 1; trigger=no
DR   NCBIfam; TIGR00511; ribulose_e2b2; 1; trigger=no
XX
KW   Carbohydrate metabolism
KW   Isomerase
XX
GO   GO:0043917; F:ribose 1,5-bisphosphate isomerase activity
GO   GO:0019323; P:pentose catabolic process
XX
FT   From: R15PI_THEKO (Q5JFM9)
FT   BINDING         20..23
FT                   /ligand="substrate"
FT   Optional; Condition: R-G-A-[GA]
FT   BINDING         135..137
FT                   /ligand="substrate"
FT   Optional; Condition: S-K-A
FT   BINDING         212..213
FT                   /ligand="substrate"
FT   Optional; Condition: N-K
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT   Condition: C
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT   Condition: D
FT   BINDING         63
FT                   /ligand="substrate"
FT   Optional; Condition: R
FT   BINDING         238
FT                   /ligand="substrate"
FT   Optional; Condition: K
XX
Size: 300-370;
Related: None;
Template: Q5JFM9; D2RW80;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.6 2023/11/09
//