ID F16PA_FLAJ1 Reviewed; 334 AA. AC A5FMJ5; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 28-JAN-2026, entry version 102. DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; DE Short=FBPase class 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 {ECO:0000255|HAMAP-Rule:MF_01855}; GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01855}; GN OrderedLocusNames=Fjoh_0533; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC OS 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga OS johnsonae). OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / RC NBRC 14942 / NCIMB 11054 / UW101; RX PubMed=19717629; DOI=10.1128/aem.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., RA Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). 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; 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 -!- 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; CP000685; ABQ03568.1; -; Genomic_DNA. DR RefSeq; WP_012022624.1; NC_009441.1. DR AlphaFoldDB; A5FMJ5; -. DR SMR; A5FMJ5; -. DR STRING; 376686.Fjoh_0533; -. DR GeneID; 31763405; -. DR KEGG; fjo:Fjoh_0533; -. DR eggNOG; COG0158; Bacteria. DR HOGENOM; CLU_039977_2_2_10; -. DR OrthoDB; 9806756at2; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000006694; Chromosome. 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 FunFam; 3.30.540.10:FF:000002; Fructose-1,6-bisphosphatase class 1; 1. DR FunFam; 3.40.190.80:FF:000001; 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; NF006778; PRK09293.1-1; 1. DR NCBIfam; NF006779; PRK09293.1-3; 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; KW Reference proteome. FT CHAIN 1..334 FT /note="Fructose-1,6-bisphosphatase class 1" FT /id="PRO_0000364555" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 120..123 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" SQ SEQUENCE 334 AA; 37172 MW; A2A441DC9FEED8A2 CRC64; MEERNKTLGE FIIENQKAFQ YSSGELSRII NSIRLAAKVV NYKVNKAGLV DIIGAAGEQN IQGEDQQKLD VYANEVFIQT LINREIVCGI ASEENDDFIT VQGSDNCHNN KYVILMDPLD GSSNIDVNVS VGTIFSVFRR ITPIGTPVTS EDFLQPGINQ VAAGYVIYGT STMLVYTTGF GVNGFTLNPA IGTFYLSHPN MKFPENGNIY SVNEGNYVHF PQGVKNYIKY CQREEEDRPY TSRYIGSLVA DFHRNMIKGG IYIYPTSSKA SKGKLRLLYE CNPMAFIAEQ AGGKATDGFG RIMEIQPTEL HQRVPFFCGS KSMVEKAEEF MAAE //