ID FBPAP_IGNH4 Reviewed; 387 AA.
AC A8A9E4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Igni_0363 {ECO:0000312|EMBL:ABU81546.1};
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
RN [2]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 mM for D-fructose 1,6-bisphosphate (when assaying the FBP
CC phosphatase activity, at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC KM=0.23 mM for triosephosphates (when assaying the FBP aldolase
CC activity in the anabolic direction, at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC Vmax=0.88 umol/min/mg enzyme for the FBP phosphatase activity (at 48
CC degrees Celsius) {ECO:0000269|PubMed:20348906};
CC Vmax=0.54 umol/min/mg enzyme for the FBP aldolase activity (at 48
CC degrees Celsius) {ECO:0000269|PubMed:20348906};
CC pH dependence:
CC Optimum pH is 8.0 for FBP phosphatase activity and 7-8.5 for the FBP
CC aldolase activity. {ECO:0000269|PubMed:20348906};
CC Temperature dependence:
CC Highly thermostable. Survives boiling for 1 hour.
CC {ECO:0000269|PubMed:20348906};
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}.
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DR EMBL; CP000816; ABU81546.1; -; Genomic_DNA.
DR RefSeq; WP_011998398.1; NC_009776.1.
DR AlphaFoldDB; A8A9E4; -.
DR SMR; A8A9E4; -.
DR STRING; 453591.Igni_0363; -.
DR GeneID; 5563123; -.
DR KEGG; iho:Igni_0363; -.
DR eggNOG; arCOG04180; Archaea.
DR HOGENOM; CLU_041630_0_0_2; -.
DR OrthoDB; 5829at2157; -.
DR PhylomeDB; A8A9E4; -.
DR BioCyc; MetaCyc:MONOMER-124174; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000262; 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..387
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437180"
FT ACT_SITE 13
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 229
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 232
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 20
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 134
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
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 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 242..243
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 266
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 266
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 287
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 287
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 348
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 387 AA; 42514 MW; 278DF5048404E211 CRC64;
MAQKTTISVI KADIGSLAGH HTVHPDCMAA ASRVLAEAKK NGVINDFYVT HVGDDLILIM
THTKGVDHPD VHGLAWEAFK KAAEVAKELG LYAAGQDLLS DAFSGNVRGL GPAAAEMEIE
ERPSEPIVIF AADKTEPGAF NLPLYKIFAD PFNTAGLVID PRLHDGFVFE VVDVFEDKGV
HLNTPEELYD LLALIGTPSR YVIRRVFRKD GKIAAVVSVE RLNLIAGKYV GKDDPVMIVR
AQSGFPAVGE VLEPFTFPHL VAGWMRGSHN GPLMPVPVRD ARPTRFDGPP RVIALGFQVK
NAKLVGPSDL FDDPAFDEAR RTANKVADYI RRHGPFMPHR LDPSEMEYTT LPQVLERLKD
RFKPVKDLPV PKVKHSEMLS GAEEAHD
//
