BSUHB_AQUAE
ID BSUHB_AQUAE Reviewed; 264 AA.
AC O67791;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase;
DE Short=FBPase/IMPase;
DE EC=3.1.3.11 {ECO:0000250|UniProtKB:Q57573};
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:Q57573};
DE AltName: Full=Inositol-1-phosphatase;
DE Short=I-1-Pase;
GN Name=suhB; Synonyms=imp2; OrderedLocusNames=aq_1983;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of myo-inositol-1(or 4)-monophosphatase (aq_1983) from
RT Aquifex aeolicus VF5.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Phosphatase with broad specificity; it can dephosphorylate
CC fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-
CC phosphate (I-1-P). {ECO:0000250|UniProtKB:Q57573}.
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:0000250|UniProtKB:Q57573};
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:0000250|UniProtKB:Q57573};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07753.1; -; Genomic_DNA.
DR PIR; C70470; C70470.
DR RefSeq; NP_214360.1; NC_000918.1.
DR RefSeq; WP_010881296.1; NC_000918.1.
DR PDB; 2PCR; X-ray; 2.60 A; A/B/C/D=1-264.
DR PDBsum; 2PCR; -.
DR AlphaFoldDB; O67791; -.
DR SMR; O67791; -.
DR STRING; 224324.aq_1983; -.
DR EnsemblBacteria; AAC07753; AAC07753; aq_1983.
DR KEGG; aae:aq_1983; -.
DR PATRIC; fig|224324.8.peg.1533; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_4_0; -.
DR InParanoid; O67791; -.
DR OMA; VHQELEF; -.
DR OrthoDB; 1741160at2; -.
DR EvolutionaryTrace; O67791; -.
DR Proteomes; UP000000798; 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 CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR022337; Inositol_monophosphatase_SuhB.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR01959; SBIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..264
FT /note="Fructose-1,6-bisphosphatase/inositol-1-
FT monophosphatase"
FT /id="PRO_0000142553"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 4..25
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:2PCR"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2PCR"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2PCR"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:2PCR"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:2PCR"
SQ SEQUENCE 264 AA; 29336 MW; 10F32D1D3B81B76A CRC64;
MENLKKYLEV AKIAALAGGQ VLKENFGKVK KENIEEKGEK DFVSYVDKTS EERIKEVILK
FFPDHEVVGE EMGAEGSGSE YRWFIDPLDG TKNYINGFPI FAVSVGLVKG EEPIVGAVYL
PYFDKLYWGA KGLGAYVNGK RIKVKDNESL KHAGVVYGFP SRSRRDISIY LNIFKDVFYE
VGSMRRPGAA AVDLCMVAEG IFDGMMEFEM KPWDITAGLV ILKEAGGVYT LVGEPFGVSD
IIAGNKALHD FILQVAKKYM EVAV
