ID D2RDW4_ARCPA Unreviewed; 371 AA. AC D2RDW4; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 56. 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=Arcpr_1256 {ECO:0000313|EMBL:ADB58308.1}; OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Archaeoglobus. OX NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB58308.1, ECO:0000313|Proteomes:UP000001901}; RN [1] {ECO:0000313|EMBL:ADB58308.1, ECO:0000313|Proteomes:UP000001901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18 RC {ECO:0000313|Proteomes:UP000001901}; RX PubMed=21304717; RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F., RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E., RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S., RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18)."; RL Stand. Genomic Sci. 2:327-346(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: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; CP001857; ADB58308.1; -; Genomic_DNA. DR RefSeq; WP_012940644.1; NC_013741.1. DR AlphaFoldDB; D2RDW4; -. DR STRING; 572546.Arcpr_1256; -. DR PaxDb; 572546-Arcpr_1256; -. DR GeneID; 8739942; -. DR KEGG; apo:Arcpr_1256; -. DR eggNOG; arCOG04180; Archaea. DR HOGENOM; CLU_041630_0_0_2; -. DR OrthoDB; 5829at2157; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000001901; 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:UP000001901}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_02067}. FT ACT_SITE 13 FT /note="Proton acceptor; for FBP phosphatase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT ACT_SITE 235 FT /note="Proton donor/acceptor; for FBP aldolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT ACT_SITE 238 FT /note="Schiff-base intermediate with DHAP; for FBP aldolase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 20 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 20 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 20 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 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 55 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 92 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 96 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 105..106 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 133 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 134 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 134 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 238 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 239 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 239 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" 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 248..249 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 272 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 272 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 293 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 293 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 354 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 371 AA; 41442 MW; 7D9DCB5A70CBA9E8 CRC64; MSEKITVSVI KADIGSVAGH STVPDEIKAL AEKKLNEAKE KGIIIDFRVF NAGDDLELVM THRKGVDSEE IHGLAWETFK ACAEKAKELK LYAAGQDLLK EAFSGNVRGL GPGVAEMEFT ERPAEPIIVF MMDKTEPGAF NLPIFRMFAD PFNTAGLVID PSMHQGFRFE VWDIKEHKRV MLSTPEEMYD LLALIGSKGR YVIKRVYPKE GGKLPADEPV AVVSTEKLFE IAGEYVGKDD PVAIVRAQSG LPAVGEVLEA FAFPHLVSGW MRGSHNGPLM PVPFRYSKCT RFDGPPRVIA AGFQLCNGKL IGPVDMFDDP AFDYTRQKAM EICDYIRRHG PFEPHRLPHE EMEYTTLPKV LKKLEARFEK I //