FBPAP_THEKO
ID FBPAP_THEKO Reviewed; 375 AA.
AC Q8NKR9; Q5JHJ3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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:12065581, ECO:0000269|PubMed:20348906};
DE EC=4.1.2.13 {ECO:0000269|PubMed:20348906};
DE AltName: Full=Fructose-1,6-bisphosphatase {ECO:0000303|PubMed:12065581};
DE Short=FBPase {ECO:0000303|PubMed:12065581};
GN Name=fbp {ECO:0000303|PubMed:12065581};
GN OrderedLocusNames=TK2164 {ECO:0000312|EMBL:BAD86353.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION AS A
RP FBPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=12065581; DOI=10.1074/jbc.m202868200;
RA Rashid N., Imanaka H., Kanai T., Fukui T., Atomi H., Imanaka T.;
RT "A novel candidate for the true fructose-1,6-bisphosphatase in archaea.";
RL J. Biol. Chem. 277:30649-30655(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15317785; DOI=10.1128/jb.186.17.5799-5807.2004;
RA Sato T., Imanaka H., Rashid N., Fukui T., Atomi H., Imanaka T.;
RT "Genetic evidence identifying the true gluconeogenic fructose-1,6-
RT bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles.";
RL J. Bacteriol. 186:5799-5807(2004).
RN [4]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
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 (PubMed:12065581, PubMed:20348906). Does not display hydrolase activity
CC against fructose 2,6-bisphosphate, fructose 6-phosphate, fructose 1-
CC phosphate, glucose 6-phosphate, and glucose 1-phosphate
CC (PubMed:12065581). Exhibits only negligible activity on inositol-1-
CC phosphate (IMP) (PubMed:15317785). Is essential for the growth of
CC T.kodakaraensis under gluconeogenic conditions (PubMed:15317785).
CC {ECO:0000269|PubMed:12065581, ECO:0000269|PubMed:15317785,
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:12065581, 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:0000305|PubMed:12065581};
CC -!- ACTIVITY REGULATION: Activity is enhanced by dithioerythritol, and is
CC slightly inhibited by fructose 2,6-bisphosphate. AMP does not inhibit
CC the enzyme activity. {ECO:0000269|PubMed:12065581}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for D-fructose 1,6-bisphosphate (when assaying the FBPase
CC activity, at 95 degrees Celsius) {ECO:0000269|PubMed:12065581};
CC Note=kcat is 17 sec(-1) for the FBPase activity (at 95 degrees
CC Celsius). kcat is 7 sec(-1) for the FBPase activity (at 85 degrees
CC Celsius). kcat is 2.9 sec(-1) for the FBPase activity (at 37 degrees
CC Celsius). {ECO:0000269|PubMed:12065581};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:12065581};
CC Temperature dependence:
CC Optimum temperature is over 95 degrees Celsius. The enzyme shows a
CC nearly linear increase in activity between 37 and 95 degrees Celsius,
CC with a 6-fold increase between these temperatures. Is highly
CC thermostable, displaying a half-life of 150 minutes in boiling water.
CC {ECO:0000269|PubMed:12065581};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000269|PubMed:15317785, ECO:0000305|PubMed:20348906}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000250|UniProtKB:F9VMT6, ECO:0000269|PubMed:12065581}.
CC -!- INDUCTION: High levels of transcripts are detected in cells grown on
CC pyruvate or amino acids, whereas no transcription is detected when
CC starch is present in the medium, revealing a sugar-repressed gene
CC expression. {ECO:0000269|PubMed:12065581}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow under
CC gluconeogenic conditions while glycolytic growth is unimpaired, and the
CC gene disruption results in the complete abolishment of intracellular
CC FBPase activity. {ECO:0000269|PubMed:15317785}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}.
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DR EMBL; AB081839; BAC10571.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD86353.1; -; Genomic_DNA.
DR RefSeq; WP_011251114.1; NC_006624.1.
DR AlphaFoldDB; Q8NKR9; -.
DR SMR; Q8NKR9; -.
DR IntAct; Q8NKR9; 1.
DR MINT; Q8NKR9; -.
DR STRING; 69014.TK2164; -.
DR EnsemblBacteria; BAD86353; BAD86353; TK2164.
DR GeneID; 3235025; -.
DR KEGG; tko:TK2164; -.
DR PATRIC; fig|69014.16.peg.2119; -.
DR eggNOG; arCOG04180; Archaea.
DR HOGENOM; CLU_041630_0_0_2; -.
DR InParanoid; Q8NKR9; -.
DR OMA; YMRRHGP; -.
DR OrthoDB; 21175at2157; -.
DR PhylomeDB; Q8NKR9; -.
DR BRENDA; 3.1.3.11; 5246.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000536; 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 PANTHER; PTHR38341; PTHR38341; 1.
DR Pfam; PF01950; FBPase_3; 1.
DR PIRSF; PIRSF015647; FBPtase_archl; 1.
DR SUPFAM; SSF111249; SSF111249; 1.
DR PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Gluconeogenesis;
KW Hydrolase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12065581"
FT CHAIN 2..375
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437185"
FT ACT_SITE 15
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 237
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 240
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 22
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 136
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 274
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 295
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
SQ SEQUENCE 375 AA; 41661 MW; 1552ED57CF19EE93 CRC64;
MAVGDKITIS VIKADIGGWP GHSRVHPQLV ETAEDVLSKA VEDGTIIDFY VATCGDDLQL
IMTHKRGVDS PDIHGLAWKA FEEATKVAKE LGLYGAGQDL LKDAFSGNVR GMGPGVAEME
ITLRKSEPVV TFHMDKTEPG AFNLPIFRMF ADPFNTAGLI IDPKMHMGFR FEVWDILEHK
RVILNTPEEL YDLLALIGAK SRYVIKRVYP KPGHPIPENE PVAVVSTEKL YEVAGEYVGK
DDPVAIVRAQ SGLPALGEVL EPFAFPHLVS GWMRGSHNGP LMPVPMHQAN PTRFDGPPRV
VALGWQISPE GKLVGPVDLF DDPAFDYARQ KALEITEYMR RHGPFEPHRL PLEEMEYTTL
PGVLKRLTDR FEPIE
