AC   MF_01855;
DC   Protein; auto
TR   HAMAP; MF_01855; -; 1; level=0
XX
Names: FBPase_class1
XX
ID   F16PA
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1;
DE            Short=FBPase class 1;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1;
GN   Name=fbp;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per subunit.;
end case
case <Property:PHOTOSYN>
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
else
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
end case
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
XX
DR   Pfam; PF00316; FBPase; 1; trigger=no
DR   PRINTS; PR00115; F16BPHPHTASE; 1; trigger=no
DR   PROSITE; PS00124; FBPASE; 1; trigger=no
XX
case <Property:PHOTOSYN>
KW   Calvin cycle
end case
KW   Carbohydrate metabolism
KW   Cytoplasm
KW   Hydrolase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
GO   GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0006094; P:gluconeogenesis
case <Property:PHOTOSYN>
GO   GO:0019253; P:reductive pentose-phosphate cycle
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: F16PA_ECOLI (P0A993)
FT   BINDING         113..116
FT                   /ligand="substrate"
FT   Optional; Condition: [DN]-G-S-S
FT   BINDING         257..259
FT                   /ligand="substrate"
FT   Optional; Condition: Y-L-Y
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Group: 1; Condition: E
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Group: 1; Condition: D
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Group: 1; Condition: D
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Group: 1; Condition: [LIV]
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Group: 1; Condition: D
FT   BINDING         275
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Group: 1; Condition: [ED]
FT   BINDING         206
FT                   /ligand="substrate"
FT   Optional; Condition: N
FT   BINDING         239
FT                   /ligand="substrate"
FT   Optional; Condition: Y
FT   BINDING         269
FT                   /ligand="substrate"
FT   Optional; Condition: K
XX
Size: 279-378;
Related: None;
Template: P0A993; Q59943;
Scope:
 Bacteria
 Archaea; Euryarchaeota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ACAM1, BRASB, PARP8, PARXL, CUPTR, DECAR, CHRFK, HALMA, LEPCP,
 METPP, NITHX, POLNA, PSET1, CUPNH, CUPMC, ALBFT, CERS1, CERS4, CERS5, CERSP,
 SALRD, XANP2
Plasmid: in NITHX, CUPNH, RHIME, CERS5, SINMW
Comments: The E.coli protein is subject to complex allosteric regulation. This
 may be the case for other members of this family.
 Conserved metal binding sites are missing in METS4 and in second and third copies
 in PARP8. Sequences are not shown in alignment.
XX
# Revision 1.26 2024/01/25
//