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HAMAP annotation rule: MF_01855

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General rule information

Accession MF_01855
Dates 23-JAN-2009 (Created)
25-NOV-2009 (Last updated, Version 4)
Data class Protein
Predictors HAMAP; MF_01855; [distribution of match scores in UniProtKB];[seed alignment for MF_01855]
Names FBPase_class1


Propagated annotation

Identifier, protein and gene names
Identifier F16PA
Protein name
RecName: Full=Fructose-1,6-bisphosphatase class 1;
Short=FBPase class 1;
EC=3.1.3.11;
AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1;
Gene name fbp
Comments
CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate.

case <FTGroup:1>
COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
end case


case <Property:PHOTOSYN>
PATHWAY: Carbohydrate biosynthesis; Calvin cycle.

else
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
end case

SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the FBPase class 1 family.
Cross-references
Pfam PF00316; FBPase; 1;
PRINTS PR00115; F16BPHPHTASE; 1;
PROSITE PS00124; FBPASE; 1;
Keywords

case <Property:PHOTOSYN>
Calvin cycle.
end case

Carbohydrate metabolism, Cytoplasm, Hydrolase.

case <FTGroup:1>
Magnesium, Metal-binding.
end case

Gene Ontology
GO:0042132; Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity.

case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case

GO:0016051; Biological process: carbohydrate biosynthetic process.

case <Property:PHOTOSYN>
GO:0019253; Biological process: reductive pentose-phosphate cycle.
end case

GO:0005737; Cellular component: cytoplasm.
Features
From: F16PA_ECOLI (P0A993)
Key     From     To       Description   Condition   FTGroup
REGION (Optional)     113     116       Substrate binding (By similarity)   [DN]-G-S-S  
REGION (Optional)     257     259       Substrate binding (By similarity)   Y-L-Y  
 
METAL     89     89       Magnesium 1 (By similarity)   E   1
METAL     110     110       Magnesium 1 (By similarity)   D   1
METAL     110     110       Magnesium 2 (By similarity)   D   1
METAL     112     112       Magnesium 1; via carbonyl oxygen (By similarity)   [LIV]   1
METAL     113     113       Magnesium 2 (By similarity)   D   1
METAL     275     275       Magnesium 2 (By similarity)   [ED]   1
 
BINDING (Optional)     206     206       Substrate (By similarity)   N  
BINDING (Optional)     239     239       Substrate (By similarity)   Y  
BINDING (Optional)     269     269       Substrate (By similarity)   K  


Additional information

Size range: 279-378 amino acids
Related UniRules: None
Template: P0A993 (F16PA_ECOLI); Q59943 (F16PA_SYNE7): [Recover all]
Scope: Bacteria
Archaea; Euryarchaeota
Fusion: Nter: None; Cter: None
Duplicate: in ACAM1, BRASB, BURP8, BURXL, CUPTR, DECAR, GRAFK, HALMA, LEPCP, METPP, NITHX, POLNA, PSEHT, RALEH, RALME, RHOFD, RHOS1, RHOS4, RHOS5, RHOSH, SALRD, XANP2
Plasmid encoded: in NITHX, RALEH, RHIME, RHOS5, 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 BURP8. Sequences are not shown in alignment.

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