ID F16A2_CERS4 Reviewed; 331 AA. AC Q3IX60; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 10-JUN-2026, entry version 108. 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}; GN OrderedLocusNames=RHOS4_33060; ORFNames=RSP_3266; OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Cereibacter. OX NCBI_TaxID=272943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC RC 12203 / NCIMB 8253 / ATH 2.4.1.; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."; RL Submitted (SEP-2005) 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; CP000144; ABA80874.1; -; Genomic_DNA. DR RefSeq; WP_011339166.1; NC_007494.2. DR AlphaFoldDB; Q3IX60; -. DR SMR; Q3IX60; -. DR STRING; 272943.RSP_3266; -. DR EnsemblBacteria; ABA80874; ABA80874; RSP_3266. DR GeneID; 3721867; -. DR GeneID; 48981331; -. DR KEGG; rsp:RSP_3266; -. DR PATRIC; fig|272943.9.peg.3693; -. DR eggNOG; COG0158; Bacteria. DR OrthoDB; 9806756at2; -. DR PhylomeDB; Q3IX60; -. DR UniPathway; UPA00116; -. DR Proteomes; UP000002703; Chromosome 2. 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-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 Calvin cycle; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; KW Metal-binding; Reference proteome. FT CHAIN 1..331 FT /note="Fructose-1,6-bisphosphatase class 1 2" FT /id="PRO_0000364667" 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 //