ID F16A1_CERS5 Reviewed; 333 AA. AC A4WW38; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 18-JUN-2025, entry version 103. DE RecName: Full=Fructose-1,6-bisphosphatase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855}; DE Short=FBPase class 1 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01855}; GN Name=fbp1 {ECO:0000255|HAMAP-Rule:MF_01855}; GN OrderedLocusNames=Rsph17025_2715; OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Cereibacter. OX NCBI_TaxID=349102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17025 / ATH 2.4.3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., RA Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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 -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle. {ECO:0000255|HAMAP- CC Rule:MF_01855}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}. 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; CP000661; ABP71602.1; -; Genomic_DNA. DR AlphaFoldDB; A4WW38; -. DR SMR; A4WW38; -. DR STRING; 349102.Rsph17025_2715; -. DR KEGG; rsq:Rsph17025_2715; -. DR eggNOG; COG0158; Bacteria. DR HOGENOM; CLU_039977_0_0_5; -. DR BioCyc; RSPH349102:G1G8M-2795-MONOMER; -. DR UniPathway; UPA00116; -. 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway. DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:TreeGrafter. DR CDD; cd00354; FBPase; 1. DR FunFam; 3.40.190.80:FF:000011; Fructose-1,6-bisphosphatase class 1; 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 Calvin cycle; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; KW Metal-binding. FT CHAIN 1..333 FT /note="Fructose-1,6-bisphosphatase class 1 1" FT /id="PRO_0000364668" FT BINDING 81 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" 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 100 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 102 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 103..106 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 263 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" SQ SEQUENCE 333 AA; 35775 MW; DA12E6B8F7D6F247 CRC64; MKPFATHPDA IPADLQDVMD RLGSVAIEVA TRIARGGIDE DLAGLCGTNT DGDGQKALDV IADDAFRAAL EGSAVRFYAS EEQEEAVTLN EAGTLALAID PLDGSSNIDT NLSVGTIFAI WPAAATAETS FLRPGSDLIA GGYIIYGPQV CLMVSFGQGT QKYVLDPGSR SFVLVDRAVK VPPASTEFAI NASNYRHWSK PIRAYIDDCV AGTEGPRGRN FNMRWLASLV AETHRILARG GVFLYPRDGR KGYEQGRLRY LYECAPIAFV ITQAGGGATD GENPILGQTP ARLHARTPFI FGSAEKVARI TAYHDLPEQE TSALFGNRGL FRS //