BSUHB_THEKO
ID BSUHB_THEKO Reviewed; 256 AA.
AC Q5JH93;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase {ECO:0000303|PubMed:15317785};
DE Short=FBPase/IMPase {ECO:0000303|PubMed:15317785};
DE EC=3.1.3.11 {ECO:0000269|PubMed:15317785};
DE EC=3.1.3.25 {ECO:0000269|PubMed:15317785};
DE AltName: Full=Inositol-1-phosphatase;
DE Short=I-1-Pase;
GN Name=suhB; Synonyms=imp {ECO:0000303|PubMed:15317785};
GN OrderedLocusNames=TK0787 {ECO:0000312|EMBL:BAD84976.1};
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DISRUPTION PHENOTYPE, NO ROLE IN GLUCONEOGENESIS, AND INDUCTION.
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).
CC -!- FUNCTION: Phosphatase with broad specificity; it can dephosphorylate
CC fructose 1,6-bisphosphate (FBP) and inositol-1-phosphate (IMP).
CC However, while possessing a high FBPase activity in vitro, does not
CC participate in gluconeogenesis in vivo. {ECO:0000269|PubMed:15317785}.
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:15317785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:15317785};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q57573};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:15317785};
CC Note=kcat is 23.4 sec(-1) for FBPase activity (at 85 degrees
CC Celsius). FBPase activity is 5-fold higher than the IMPase activity.
CC {ECO:0000269|PubMed:15317785};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15317785}.
CC -!- INDUCTION: Constitutively expressed, at a very weak level.
CC {ECO:0000269|PubMed:15317785}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene does not lead to any
CC detectable phenotypic changes regarding the growth under gluconeogenic
CC conditions (medium supplemented with pyruvate) and glycolytic
CC conditions (medium supplemented with soluble starch).
CC {ECO:0000269|PubMed:15317785}.
CC -!- MISCELLANEOUS: Is not able to complement the defect of the fbp deletion
CC under gluconeogenic conditions, probably due to insufficient
CC transcription. {ECO:0000269|PubMed:15317785}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000305}.
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DR EMBL; AP006878; BAD84976.1; -; Genomic_DNA.
DR RefSeq; WP_011249738.1; NC_006624.1.
DR AlphaFoldDB; Q5JH93; -.
DR SMR; Q5JH93; -.
DR STRING; 69014.TK0787; -.
DR EnsemblBacteria; BAD84976; BAD84976; TK0787.
DR GeneID; 3233838; -.
DR KEGG; tko:TK0787; -.
DR PATRIC; fig|69014.16.peg.767; -.
DR eggNOG; arCOG01349; Archaea.
DR HOGENOM; CLU_044118_5_0_2; -.
DR InParanoid; Q5JH93; -.
DR OMA; RWGDERY; -.
DR OrthoDB; 99063at2157; -.
DR PhylomeDB; Q5JH93; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..256
FT /note="Fructose-1,6-bisphosphatase/inositol-1-
FT monophosphatase"
FT /id="PRO_0000437186"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
SQ SEQUENCE 256 AA; 27985 MW; BCD8E27C3FB5769B CRC64;
MEFNWSEIAL NTAKELEEKI MPLFGTKKAG ENVGTNVSGD VTKYVDKVAE DIILKRLVPL
GVNVVSEEVG TVDSGSDYTV VVDPLDGSYN FSAGIPIFAF SLGIFKGKKP VYGAIYEFLP
ENFYEAKPGK GAYLNGERIR VNEPEPGKEA LSFYTRGRCL GLVKKVKRVR VLGAIAVELA
YVARGSLDGV FDIRNYVRPT DVAAGVLLVR EAGGIVTDER GREFEVKLSA TEKTNIIAVA
NERLLNTILE AMKDEP
