BSUHB_THEMA
ID BSUHB_THEMA Reviewed; 256 AA.
AC O33832;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase;
DE Short=FBPase/IMPase;
DE EC=3.1.3.11 {ECO:0000269|PubMed:11062561};
DE EC=3.1.3.25 {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561};
DE AltName: Full=Inositol-1-phosphatase;
DE Short=I-1-Pase;
GN Name=suhB; OrderedLocusNames=TM_1415;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9720201; DOI=10.1007/s002530051256;
RA Liebl W., Brem D., Gotschlich A.;
RT "Analysis of the gene for beta-fructosidase (invertase, inulinase) of the
RT hyperthermophilic bacterium Thermotoga maritima, and characterisation of
RT the enzyme expressed in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 50:55-64(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP FUNCTION AS IMPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=10508089; DOI=10.1128/aem.65.10.4559-4567.1999;
RA Chen L., Roberts M.F.;
RT "Characterization of a tetrameric inositol monophosphatase from the
RT hyperthermophilic bacterium Thermotoga maritima.";
RL Appl. Environ. Microbiol. 65:4559-4567(1999).
RN [4]
RP FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, AND KINETIC
RP PARAMETERS.
RX PubMed=11062561; DOI=10.1038/80968;
RA Stec B., Yang H., Johnson K.A., Chen L., Roberts M.F.;
RT "MJ0109 is an enzyme that is both an inositol monophosphatase and the
RT 'missing' archaeal fructose-1,6-bisphosphatase.";
RL Nat. Struct. Biol. 7:1046-1050(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RX PubMed=17419729; DOI=10.1111/j.0014-2956.2007.05779.x;
RA Stieglitz K.A., Roberts M.F., Li W., Stec B.;
RT "Crystal structure of the tetrameric inositol 1-phosphate phosphatase
RT (TM1415) from the hyperthermophile, Thermotoga maritima.";
RL FEBS J. 274:2461-2469(2007).
CC -!- FUNCTION: Phosphatase with broad specificity; it can dephosphorylate
CC fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate
CC (I-1-P) but displaying a 20-fold higher rate of hydrolysis of D-I-1-P
CC than of the L isomer, 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol
CC phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-
CC phosphate, fructose-6-phosphate, 5'-AMP and NAD(+). May be involved in
CC the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}.
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:11062561};
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:10508089, ECO:0000269|PubMed:11062561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10508089};
CC -!- ACTIVITY REGULATION: In contrast to mammalian I-1-P phosphatases, is
CC only weakly inhibited by Li(+), since 50% inhibitory concentration for
CC Li(+) is about 100 mM, and the Li(+) concentration required to totally
CC abolish I-1-Pase activity is 1 M.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.145 mM for DL-inositol-1-phosphate (at 95 degrees Celsius)
CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561};
CC KM=0.126 mM for D-inositol-1-phosphate (at 95 degrees Celsius)
CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561};
CC KM=0.460 mM for inositol-2-phosphate (at 95 degrees Celsius)
CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561};
CC Vmax=443 umol/min/mg enzyme with D-inositol-1-phosphate as substrate
CC (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089,
CC ECO:0000269|PubMed:11062561};
CC Vmax=23 umol/min/mg enzyme with L-inositol-1-phosphate as substrate
CC (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089,
CC ECO:0000269|PubMed:11062561};
CC Vmax=5.8 umol/min/mg enzyme with inositol-2-phosphate as substrate
CC (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089,
CC ECO:0000269|PubMed:11062561};
CC Note=kcat is 207 sec(-1) for IMPase activity (at 95 degrees Celsius)
CC and 268 sec(-1) for FBPase activity (at 95 degrees Celsius).
CC {ECO:0000269|PubMed:11062561};
CC Temperature dependence:
CC Thermostable. No loss of IMPase activity after incubation at 85
CC degrees Celsius for 30 minutes. Heating at 100 degrees Celsius for 10
CC minutes results in a loss of about 20 to 25% of the activity, and 30
CC minutes at this temperature inactivate about 70% of the activity.
CC {ECO:0000269|PubMed:10508089};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10508089,
CC ECO:0000269|PubMed:17419729}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD36486.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ001073; CAA04517.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36486.1; ALT_FRAME; Genomic_DNA.
DR PIR; E72255; E72255.
DR PIR; T50642; T50642.
DR RefSeq; NP_229216.1; NC_000853.1.
DR RefSeq; WP_004081652.1; NZ_CP011107.1.
DR PDB; 2P3N; X-ray; 2.20 A; A/B/C/D=1-256.
DR PDB; 2P3V; X-ray; 2.40 A; A/B/C/D=1-256.
DR PDBsum; 2P3N; -.
DR PDBsum; 2P3V; -.
DR AlphaFoldDB; O33832; -.
DR SMR; O33832; -.
DR STRING; 243274.THEMA_07245; -.
DR EnsemblBacteria; AAD36486; AAD36486; TM_1415.
DR KEGG; tma:TM1415; -.
DR PATRIC; fig|243274.5.peg.1426; -.
DR eggNOG; COG0483; Bacteria.
DR InParanoid; O33832; -.
DR OMA; RVDGYWE; -.
DR OrthoDB; 1741160at2; -.
DR BioCyc; MetaCyc:MON-5063; -.
DR BRENDA; 3.1.3.25; 6331.
DR SABIO-RK; O33832; -.
DR EvolutionaryTrace; O33832; -.
DR Proteomes; UP000008183; 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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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_0000142574"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17419729"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17419729"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17419729"
FT BINDING 82..84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 2..21
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:2P3N"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:2P3N"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:2P3N"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2P3N"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2P3V"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2P3N"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:2P3N"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:2P3N"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2P3N"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2P3N"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2P3N"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:2P3N"
SQ SEQUENCE 256 AA; 28647 MW; 550C15FEEA50B8DC CRC64;
MDRLDFSIKL LRKVGHLLMI HWGRVDNVEK KTGFKDIVTE IDREAQRMIV DEIRKFFPDE
NIMAEEGIFE KGDRLWIIDP IDGTINFVHG LPNFSISLAY VENGEVKLGV VHAPALNETL
YAEEGSGAFF NGERIRVSEN ASLEECVGST GSYVDFTGKF IERMEKRTRR IRILGSAALN
AAYVGAGRVD FFVTWRINPW DIAAGLIIVK EAGGMVTDFS GKEANAFSKN FIFSNGLIHD
EVVKVVNEVV EEIGGK
