ID F16A1_PARXL Reviewed; 338 AA. AC Q13V64; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 28-JAN-2026, entry version 107. 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=Bxeno_A3487; ORFNames=Bxe_A0920; OS Paraburkholderia xenovorans (strain LB400). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T., RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome RT shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). 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; CP000270; ABE32025.1; -; Genomic_DNA. DR RefSeq; WP_007180818.1; NC_007951.1. DR AlphaFoldDB; Q13V64; -. DR SMR; Q13V64; -. DR STRING; 266265.Bxe_A0920; -. DR KEGG; bxb:DR64_3083; -. DR KEGG; bxe:Bxe_A0920; -. DR eggNOG; COG0158; Bacteria. DR OrthoDB; 9806756at2; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000001817; Chromosome 1. 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:000006; Fructose-1,6-bisphosphatase class 1; 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 NCBIfam; NF006778; PRK09293.1-1; 1. DR NCBIfam; NF006779; PRK09293.1-3; 1. 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. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1..338 FT /note="Fructose-1,6-bisphosphatase class 1 1" FT /id="PRO_0000364506" FT BINDING 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 116 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 116 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 118 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 119..122 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 210 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 276 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 282 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" SQ SEQUENCE 338 AA; 37622 MW; 60E172A370B1D6FD CRC64; MALQRRTTLT KYLIEQQRET NNLPADLRLL IEVVARACKA ISYHVSKGAL GDALGTAGSE NVQGEVQKKL DILSNEILLE ANEWGGNLAG MASEEMEQFF PIPANYPKGE YLLVFDPLDG SSNIDVNVSI GTIFSVLRCP DGQQPTEQSF LQPGTQQVAA GYAVYGPQTV LVLTTGNGVN CFTLDRELGS WVLTQSDMRI PVETREYAIN ASNERHWYPP VQQYIGELKD GKEGSRQSDF NMRWIASMVA DVHRILNRGG IFMYPADKRT PDKPGKLRLM YEANPMAFIV EQAGGAATNG EKRILDIQPK SLHERVAVFL GSKNEVDRVT RYHLETKK //