ID F16A2_CERSP Reviewed; 331 AA. AC P22780; Q79D81; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 10-JUN-2026, entry version 111. DE RecName: Full=Fructose-1,6-bisphosphatase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855}; DE Short=FBPase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855}; DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855}; DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855}; GN Name=fbp2 {ECO:0000255|HAMAP-Rule:MF_01855}; Synonyms=fbpB; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2175647; DOI=10.1021/bi00487a014; RA Gibson J.L., Chen J.-H., Tower P.A., Tabita F.R.; RT "The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form RT part of a large operon in Rhodobacter sphaeroides: primary structure and RT insertional mutagenesis analysis."; RL Biochemistry 29:8085-8093(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RC STRAIN=HR; RX PubMed=7961502; DOI=10.1128/jb.176.23.7299-7308.1994; RA Xu H.H., Tabita F.R.; RT "Positive and negative regulation of sequences upstream of the form II cbb RT CO2 fixation operon of Rhodobacter sphaeroides."; RL J. Bacteriol. 176:7299-7308(1994). 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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01855}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01855}; CC -!- ACTIVITY REGULATION: Fructose-1,6-bisphosphatase II is not light- CC activated. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- MISCELLANEOUS: There are two genes for FBPase in R.sphaeroides. CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP- CC Rule:MF_01855}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02922; AAA26105.1; -; Genomic_DNA. DR EMBL; U12430; AAA65078.1; -; Genomic_DNA. DR PIR; A35819; A35819. DR RefSeq; WP_011339166.1; NZ_CBCSES010000004.1. DR AlphaFoldDB; P22780; -. DR SMR; P22780; -. DR GeneID; 48981331; -. DR UniPathway; UPA00138; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:TreeGrafter. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:TreeGrafter. DR GO; GO:0006000; P:fructose metabolic process; IEA:TreeGrafter. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:TreeGrafter. DR CDD; cd00354; FBPase; 1. DR Gene3D; 3.40.190.80; -; 1. DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1. DR HAMAP; MF_01855; FBPase_class1; 1. DR InterPro; IPR044015; FBPase_C_dom. DR InterPro; IPR000146; FBPase_class-1. DR InterPro; IPR033391; FBPase_N. DR InterPro; IPR028343; FBPtase. DR InterPro; IPR020548; Fructose_bisphosphatase_AS. DR NCBIfam; NF006780; PRK09293.1-4; 1. DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1. DR PANTHER; PTHR11556:SF35; SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC; 1. DR Pfam; PF00316; FBPase; 1. DR Pfam; PF18913; FBPase_C; 1. DR PIRSF; PIRSF500210; FBPtase; 1. DR PIRSF; PIRSF000904; FBPtase_SBPase; 1. DR PRINTS; PR00115; F16BPHPHTASE. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR PROSITE; PS00124; FBPASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding. FT CHAIN 1..331 FT /note="Fructose-1,6-bisphosphatase class 1 2" FT /id="PRO_0000200488" FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 100 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 101..104 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 101 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" SQ SEQUENCE 331 AA; 35256 MW; 500EB63E9BBECD13 CRC64; MAIELEDLGL SPDVADVMQR LARVGAGIAR IISRNGLERD LGAGVGTNAG GDGQKALDVI ADDAFRAALE GSAVAYYASE EQDEVVTLGE GSLALAIDPL DGSSNIDVNV SIGTIFSIFP AAAGPEASFL RPGTEQIAGG YIIYGPQCAL VCSFGQGVQH WVLDLDAGIF RRMPDIRPLP AETSEFAINA SNYRHWPQPI RAFVDDLVAG AEGPRGKNFN MRWIASLVAE THRILMRGGV FLYPGDERKG YERGRLRHVY ECAPIAFLIA NVGGGATDGC ADILTALPDR LHARTPFVFG CASKVARVAA YHDLACEETS ALFGSRGLFR S //