FBP_PYRFU
ID FBP_PYRFU Reviewed; 254 AA.
AC Q8TZH9; E7FHX0; Q7LWG3;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Fructose-1,6-bisphosphatase {ECO:0000303|PubMed:12029059};
DE Short=FBPase {ECO:0000305};
DE EC=3.1.3.11 {ECO:0000269|PubMed:12029059};
GN Name=fbpA {ECO:0000303|PubMed:12029059};
GN Synonyms=fbp {ECO:0000312|EMBL:AAM48105.1};
GN OrderedLocusNames=PF2014 {ECO:0000312|EMBL:AAL82138.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=12029059; DOI=10.1128/jb.184.12.3401-3405.2002;
RA Verhees C.H., Akerboom J., Schiltz E., de Vos W.M., van der Oost J.;
RT "Molecular and biochemical characterization of a distinct type of fructose-
RT 1,6-bisphosphatase from Pyrococcus furiosus.";
RL J. Bacteriol. 184:3401-3405(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3] {ECO:0007744|PDB:1XI6}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-254.
RG Southeast collaboratory for structural genomics (SECSG);
RA Zhao M., Chang J.C., Zhou W., Chen L., Horanyi P., Xu H., Yang H.,
RA Liu Z.-J., Habel J.E., Lee D., Chang S.-H., Rose J.P., Wang B.-C.;
RT "Extragenic suppressor from Pyrococcus furiosus Pfu-1862794-001.";
RL Submitted (SEP-2004) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of D-fructose 1,6-bisphosphate to D-
CC fructose 6-phosphate. In vitro, has also weak activity with inositol-1-
CC phosphate, glucose-1-phosphate and glycerol-2-phosphate.
CC {ECO:0000269|PubMed:12029059}.
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:12029059};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12029059};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+), ADP, ATP and glucose-6-
CC phosphate. {ECO:0000269|PubMed:12029059}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for fructose 1,6-bisphosphate (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:12029059};
CC KM=0.31 mM for fructose 1,6-bisphosphate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:12029059};
CC Vmax=12.2 umol/min/mg enzyme (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:12029059};
CC Vmax=0.72 umol/min/mg enzyme (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:12029059};
CC Temperature dependence:
CC Optimum temperature is approximately 100 degrees Celsius.
CC {ECO:0000269|PubMed:12029059};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12029059}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000305|PubMed:12029059}.
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DR EMBL; AF453319; AAM48105.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL82138.1; -; Genomic_DNA.
DR RefSeq; WP_011013159.1; NC_018092.1.
DR PDB; 1XI6; X-ray; 2.80 A; A=2-254.
DR PDBsum; 1XI6; -.
DR AlphaFoldDB; Q8TZH9; -.
DR SMR; Q8TZH9; -.
DR STRING; 186497.PF2014; -.
DR EnsemblBacteria; AAL82138; AAL82138; PF2014.
DR GeneID; 41713840; -.
DR KEGG; pfu:PF2014; -.
DR PATRIC; fig|186497.12.peg.2091; -.
DR eggNOG; arCOG01349; Archaea.
DR HOGENOM; CLU_044118_5_0_2; -.
DR OMA; RWGDERY; -.
DR OrthoDB; 99063at2157; -.
DR PhylomeDB; Q8TZH9; -.
DR BRENDA; 3.1.3.11; 5243.
DR EvolutionaryTrace; Q8TZH9; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..254
FT /note="Fructose-1,6-bisphosphatase"
FT /id="PRO_0000442420"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q57573"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1XI6"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1XI6"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1XI6"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:1XI6"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1XI6"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1XI6"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:1XI6"
SQ SEQUENCE 254 AA; 27928 MW; 4849088A9936D272 CRC64;
MKLKFWREVA IDIISDFETT IMPFFGNPDG GKLVKISPSG DETKLVDKLA EDLILSRITE
LGVNVVSEEV GVIDNESEYT VIVDPLDGSY NFIAGIPFFA LSLAVFKKDK PIYAIIYEPM
TERFFEGIPG EGAFLNGKRI KVRKTPDEKP SISFYSRGKG HEIVKHVKRT RTLGAIALEL
AYLAMGALDG VVDVRKYVRP TDIAAGTIIA KEAGALIKDS AGKDIDISFN ATDRLDVIAV
NSEELLKTIL SLLE
