ID F0LKH3_THEBM Unreviewed; 374 AA. AC F0LKH3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 51. DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000256|ARBA:ARBA00018635, ECO:0000256|HAMAP-Rule:MF_02067}; DE Short=FBP A/P {ECO:0000256|HAMAP-Rule:MF_02067}; DE Short=FBP aldolase/phosphatase {ECO:0000256|HAMAP-Rule:MF_02067}; DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093, ECO:0000256|HAMAP-Rule:MF_02067}; DE EC=4.1.2.13 {ECO:0000256|HAMAP-Rule:MF_02067}; GN Name=fbp {ECO:0000256|HAMAP-Rule:MF_02067}; GN OrderedLocusNames=TERMP_01832 {ECO:0000313|EMBL:ADT84807.1}; OS Thermococcus barophilus (strain DSM 11836 / MP). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT84807.1, ECO:0000313|Proteomes:UP000007478}; RN [1] {ECO:0000313|EMBL:ADT84807.1, ECO:0000313|Proteomes:UP000007478} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478}; RX PubMed=21217005; DOI=10.1128/JB.01490-10; RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.; RT "Complete genome sequence of the hyperthermophilic, piezophilic, RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP."; RL J. Bacteriol. 193:1481-1482(2011). 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:0000256|HAMAP-Rule:MF_02067}. 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:0000256|ARBA:ARBA00001273, ECO:0000256|HAMAP- CC Rule:MF_02067}; 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:0000256|HAMAP-Rule:MF_02067}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_02067}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|HAMAP-Rule:MF_02067}. CC -!- SUBUNIT: Homooctamer; dimer of tetramers. CC {ECO:0000256|ARBA:ARBA00011820, ECO:0000256|HAMAP-Rule:MF_02067}. 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:0000256|HAMAP-Rule:MF_02067}. CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family. CC {ECO:0000256|ARBA:ARBA00010693, ECO:0000256|HAMAP-Rule:MF_02067}. 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; CP002372; ADT84807.1; -; Genomic_DNA. DR RefSeq; WP_013468103.1; NC_014804.1. DR AlphaFoldDB; F0LKH3; -. DR GeneID; 10042148; -. DR KEGG; tba:TERMP_01832; -. DR PATRIC; fig|391623.17.peg.1831; -. DR eggNOG; arCOG04180; Archaea. DR HOGENOM; CLU_041630_0_0_2; -. DR OrthoDB; 5829at2157; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000007478; 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 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_02067}; KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP- KW Rule:MF_02067}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02067}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02067}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_02067}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_02067}; Reference proteome {ECO:0000313|Proteomes:UP000007478}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_02067}. FT ACT_SITE 15 FT /note="Proton acceptor; for FBP phosphatase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT ACT_SITE 237 FT /note="Proton donor/acceptor; for FBP aldolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT ACT_SITE 240 FT /note="Schiff-base intermediate with DHAP; for FBP aldolase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 15 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 22 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 22 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 56 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 56 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 57 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 94 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 107..108 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 135 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 136 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 136 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 250..251 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 274 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 274 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 295 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 295 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:0000256|HAMAP-Rule:MF_02067" FT BINDING 357 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:0000256|HAMAP-Rule:MF_02067" SQ SEQUENCE 374 AA; 41824 MW; 7AB4EF3D0E0E2D09 CRC64; MAVGEKITIS VIKADIGGWP GHHKVHPALI EKAREILSKA KEEGTIIDFH VTYCGDDLQL IMTHKKGTDS PDIHGLAWET FKEATKTAKE LGLYGAGQDL LKDAFSGNIR GMGPGAAEME ITIRKSEPIV TFHMDKTEPG AFNLPIFRMF ADPFNTAGLV IDPNMHMGFR FEIWDIREHK RVIMNSPEEM YDILALIGAK SRYVIKRVFP KEGHKLPKDE PVAVVSTEKL YEIAGEYVGK DDPVAIVRAQ SGLPALGEVL EPFAFPHLVS GWMRGSHNGP IMPVPLKYAT PSRFDGPPRA VALGWQISPE GKLIGPVDLF DDPAFDWARQ KALEITEYMR RHGPFEPHRL PLEEMEYTTL PGVLEKLKDR FEPL //