ID F16PA_PARL1 Reviewed; 343 AA. AC A7HYA5; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=Plav_3283; OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Parvibaculaceae; Parvibaculum. OX NCBI_TaxID=402881; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966; RX PubMed=22675581; DOI=10.4056/sigs.2215005; RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S., RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L., RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.; RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS- RT 1(T))."; RL Stand. Genomic Sci. 5:298-310(2011). 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; CP000774; ABS64888.1; -; Genomic_DNA. DR RefSeq; WP_012112216.1; NC_009719.1. DR AlphaFoldDB; A7HYA5; -. DR SMR; A7HYA5; -. DR STRING; 402881.Plav_3283; -. DR KEGG; pla:Plav_3283; -. DR eggNOG; COG0158; Bacteria. DR HOGENOM; CLU_039977_0_0_5; -. DR OrthoDB; 9806756at2; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000006377; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. 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 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..343 FT /note="Fructose-1,6-bisphosphatase class 1" FT /id="PRO_0000364620" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855" FT BINDING 115 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..119 FT /ligand="substrate" 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 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 343 AA; 38228 MW; 5C74BD12671D485A CRC64; MSQRTLTQFL IEQQRKEAAL PAQLRLLVEI VARACKTISH CVNKGALGGM LGNLTSENVQ GEVQKKLDVI ANEKLLEANE WGGHLAAMAS EEMETIHLIP NRYPKGEYLL LFDPIDGSSN IDVDLSVGTI FSVLTAPEDV SGRAVTEADF LQPGRKQVAA GYAIYGPQTL LILSVGTGVY EFALDREMGS WVLTNERIRI PSGNREFAIN MSNMRHWAPP VRRYIDECLA GTTGPREANF NMRWTASMVA DIHRILKRGG IFMYPWDARE PDRAGKLRLM YEANPMGFLI EQAGGMAFDG NHRILDIEPK ALHQRVGVVM GDRDEVKRVV QYHHDANLAK QTA //