ID D5U307_THEAM Unreviewed; 381 AA. AC D5U307; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 58. 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=Tagg_1241 {ECO:0000313|EMBL:ADG91507.1}; OS Thermosphaera aggregans (strain DSM 11486 / M11TL). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Thermosphaera. OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG91507.1, ECO:0000313|Proteomes:UP000002376}; RN [1] {ECO:0000313|EMBL:ADG91507.1, ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX PubMed=21304709; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T., RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [2] {ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX DOI=10.4056/sigs.821804; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T., RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TLT)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11486; RG US DOE Joint Genome Institute (JGI-PGF); RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H., RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P., RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. 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; CP001939; ADG91507.1; -; Genomic_DNA. DR RefSeq; WP_013130100.1; NC_014160.1. DR AlphaFoldDB; D5U307; -. DR STRING; 633148.Tagg_1241; -. DR GeneID; 9166284; -. DR KEGG; tag:Tagg_1241; -. DR eggNOG; arCOG04180; Archaea. DR HOGENOM; CLU_041630_0_0_2; -. DR OrthoDB; 5829at2157; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000002376; 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:UP000002376}; 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 230 FT /note="Proton donor/acceptor; for FBP aldolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT ACT_SITE 233 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 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 234 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 234 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 235 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 235 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 243..244 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 267 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 267 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 288 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067" FT BINDING 288 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 349 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 381 AA; 42534 MW; BAA86C23921BD26C CRC64; MGDKITLSII KADVGSIAGH HMPHPDQLAA ATKILAEAKQ KDIIIDFYVT HVGDDIQLIM THRKGVDHPD IHGLAWEAFK SATKVAKELK LYAAGQDLLS EAFSGNVRGM GPGVAELEME EREAEPVITF HADKTEPGAF NMPIYRIFAD PFNTAGLVID PKMHDGFIFE VYDVFEGRSV LMKTPEESYD VLALIGTPGR YIVRRVYRKS DNLLAAVVSV ERLNLTAGRY VGKDDPVAIV RAQHGLPAVG EVLEPFSFPH LVAGWMRGSH HGPLMPVPMR YAKVTRFDGP PRIIALGWNI SKGRLIGPVD LFDDVAFDET RRLAEMIAEY MRRHGPFMPH RLGPEEMEYT TLPSVLEKLK DRFVKTEEVK VVKKHSDLLS H //