ID FBPAP_METS5 Reviewed; 383 AA. AC A4YIZ5; DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000303|PubMed:20348906}; DE Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067}; DE Short=FBP aldolase/phosphatase {ECO:0000303|PubMed:20348906}; DE EC=3.1.3.11 {ECO:0000269|PubMed:20348906}; DE EC=4.1.2.13 {ECO:0000269|PubMed:20348906}; GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067}; GN OrderedLocusNames=Msed_2259 {ECO:0000312|EMBL:ABP96397.1}; OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 OS / TH2). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Metallosphaera. OX NCBI_TaxID=399549; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2; RX PubMed=18083856; DOI=10.1128/aem.02019-07; RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.; RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic RT archaeon Metallosphaera sedula provides insights into bioleaching- RT associated metabolism."; RL Appl. Environ. Microbiol. 74:682-692(2008). RN [2] RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY. RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2; RX PubMed=20348906; DOI=10.1038/nature08884; RA Say R.F., Fuchs G.; RT "Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral RT gluconeogenic enzyme."; RL Nature 464:1077-1081(2010). CC -!- FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol CC condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3- CC phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the CC dephosphorylation of FBP to fructose-6-phosphate (F6P). CC {ECO:0000269|PubMed:20348906}. 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:0000269|PubMed:20348906}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC Evidence={ECO:0000269|PubMed:20348906}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:F9VMT6}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000305|PubMed:20348906}. CC -!- SUBUNIT: Homooctamer; dimer of tetramers. CC {ECO:0000250|UniProtKB:F9VMT6}. CC -!- DOMAIN: Consists of a single catalytic domain, but remodels its active- CC site architecture via a large structural change to exhibit dual CC activities. {ECO:0000250|UniProtKB:F9VMT6}. CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family. CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}. 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; CP000682; ABP96397.1; -; Genomic_DNA. DR AlphaFoldDB; A4YIZ5; -. DR SMR; A4YIZ5; -. DR STRING; 399549.Msed_2259; -. DR KEGG; mse:Msed_2259; -. DR eggNOG; arCOG04180; Archaea. DR HOGENOM; CLU_041630_0_0_2; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000242; Chromosome. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR HAMAP; MF_02067; FBP_aldolase_phosphatase; 1. DR InterPro; IPR002803; FBPase_V. DR InterPro; IPR036076; FBPase_V_sf. DR NCBIfam; NF041126; FBP_aldo_phos; 1. DR PANTHER; PTHR38341; FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE/PHOSPHATASE; 1. DR PANTHER; PTHR38341:SF1; FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE_PHOSPHATASE; 1. DR Pfam; PF01950; FBPase_3; 1. DR PIRSF; PIRSF015647; FBPtase_archl; 1. DR SUPFAM; SSF111249; Sulfolobus fructose-1,6-bisphosphatase-like; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase; Magnesium; KW Metal-binding; Reference proteome; Schiff base. FT CHAIN 1..383 FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase" FT /id="PRO_0000437181" FT REGION 361..383 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 11 FT /note="Proton acceptor; for FBP phosphatase activity" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT ACT_SITE 228 FT /note="Proton donor/acceptor; for FBP aldolase activity" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT ACT_SITE 231 FT /note="Schiff-base intermediate with DHAP; for FBP aldolase FT activity" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 11 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 18 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 18 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 90 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 103..104 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 131 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 132 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 132 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 241..242 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 265 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 265 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 286 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 286 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" FT BINDING 347 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:F9VMT6" SQ SEQUENCE 383 AA; 42534 MW; 87D5E21A3CA547C3 CRC64; MRSTVSVIKA DIGSLAGHHV VHPDTMAAAN RVLAEAKRQG IILDYYITNV GDDLELIMSH TRGELDTKVH ETAWDAFKEA TKVSKELGLY AAGQDLLSDS FSGNLKGMGP GIAELDIEER PSEPIAIFMA DKTEPGAFNL PLYKMFADPF NTAGLVIDPT MNEGFKFEVL DVYEGQSVVL NSPEEMYSLL GLIGTPARYV IRRVYRKADN MIGSVTSIER LNLIAGKYVG KDDPVLIVRL QHGFPALGEA LEAFSFPYLV PGWMRGSHYG PIMPVSQRDA KATRFDGPPR LIGLGFNVKN GKLTGPSDLF DDPAFDETRR MASVITDYMR RHGPFMPHRL EPTEMEYTTL PTLIEKLKPR FKKEEDVKKA KPSVYTSKDQ GMD //