ID BSUHB_METJA Reviewed; 252 AA.
AC Q57573;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase;
DE Short=FBPase/IMPase;
DE EC=3.1.3.11 {ECO:0000269|PubMed:9647837};
DE EC=3.1.3.25 {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
DE AltName: Full=Inositol-1-phosphatase;
DE Short=I-1-Pase;
GN Name=suhB; OrderedLocusNames=MJ0109;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS IMPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=9647837; DOI=10.1128/aem.64.7.2609-2615.1998;
RA Chen L., Roberts M.F.;
RT "Cloning and expression of the inositol monophosphatase gene from
RT Methanococcus jannaschii and characterization of the enzyme.";
RL Appl. Environ. Microbiol. 64:2609-2615(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND METAL
RP IONS, FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH MYO-INOSITOL
RP PHOSPHATE; MYO-INOSITOL AND METAL IONS.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=11170378; DOI=10.1021/bi0016422;
RA Johnson K.A., Chen L., Yang H., Roberts M.F., Stec B.;
RT "Crystal structure and catalytic mechanism of the MJ0109 gene product: a
RT bifunctional enzyme with inositol monophosphatase and fructose 1,6-
RT bisphosphatase activities.";
RL Biochemistry 40:618-630(2001).
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), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-
CC phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate,
CC NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique
CC osmolyte, di-myo-inositol 1,1-phosphate. {ECO:0000269|PubMed:11062561,
CC ECO:0000269|PubMed:9647837}.
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:11062561, ECO:0000269|PubMed:9647837};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9647837};
CC -!- ACTIVITY REGULATION: IMPase activity is inhibited by Ca(2+) and Zn(2+).
CC In contrast to mammalian I-1-P phosphatases, is not inhibited by Li(+)
CC up to 100 mM. {ECO:0000269|PubMed:9647837}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.091 mM for inositol-1-phosphate (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC KM=0.038 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC Vmax=9.3 umol/min/mg enzyme for IMPase activity (at 85 degrees
CC Celsius) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC Note=kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius)
CC and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).;
CC Temperature dependence:
CC Is thermostable. After incubation at 85 degrees Celsius for 30
CC minutes, more than 95% of I-1-Pase activity remains.
CC {ECO:0000269|PubMed:9647837};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11062561,
CC ECO:0000269|PubMed:9647837}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000305}.
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DR EMBL; L77117; AAB98091.1; -; Genomic_DNA.
DR PIR; E64313; E64313.
DR RefSeq; WP_010869601.1; NC_000909.1.
DR PDB; 1DK4; X-ray; 2.60 A; A/B=1-252.
DR PDB; 1G0H; X-ray; 2.30 A; A/B=1-252.
DR PDB; 1G0I; X-ray; 2.40 A; A/B=1-252.
DR PDBsum; 1DK4; -.
DR PDBsum; 1G0H; -.
DR PDBsum; 1G0I; -.
DR AlphaFoldDB; Q57573; -.
DR SMR; Q57573; -.
DR STRING; 243232.MJ_0109; -.
DR PaxDb; 243232-MJ_0109; -.
DR EnsemblBacteria; AAB98091; AAB98091; MJ_0109.
DR GeneID; 1450950; -.
DR KEGG; mja:MJ_0109; -.
DR eggNOG; arCOG01349; Archaea.
DR HOGENOM; CLU_044118_5_0_2; -.
DR InParanoid; Q57573; -.
DR OrthoDB; 58111at2157; -.
DR PhylomeDB; Q57573; -.
DR BioCyc; MetaCyc:MONOMER-5062; -.
DR BRENDA; 3.1.3.108; 3260.
DR BRENDA; 3.1.3.11; 3260.
DR BRENDA; 3.1.3.25; 3260.
DR SABIO-RK; Q57573; -.
DR EvolutionaryTrace; Q57573; -.
DR Proteomes; UP000000805; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006020; P:inositol metabolic process; 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 CDD; cd01515; Arch_FBPase_1; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
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..252
FT /note="Fructose-1,6-bisphosphatase/inositol-1-
FT monophosphatase"
FT /id="PRO_0000142580"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:11062561,
FT ECO:0000305|PubMed:11170378"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:11062561,
FT ECO:0000305|PubMed:11170378"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:11062561,
FT ECO:0000305|PubMed:11170378"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:11062561,
FT ECO:0000305|PubMed:11170378"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170378"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:11062561,
FT ECO:0000305|PubMed:11170378"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170378"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170378"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170378"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:11062561,
FT ECO:0000305|PubMed:11170378"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1G0H"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1G0H"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 97..115
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1G0H"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1G0I"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1G0I"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1DK4"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:1G0H"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1G0H"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1G0H"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:1G0H"
SQ SEQUENCE 252 AA; 28578 MW; 3ED5B4401075EE6E CRC64;
MKWDEIGKNI AKEIEKEILP YFGRKDKSYV VGTSPSGDET EIFDKISEDI ALKYLKSLNV
NIVSEELGVI DNSSEWTVVI DPIDGSFNFI NGIPFFAFCF GVFKNNEPYY GLTYEFLTKS
FYEAYKGKGA YLNGRKIKVK DFNPNNIVIS YYPSKKIDLE KLRNKVKRVR IFGAFGLEMC
YVAKGTLDAV FDVRPKVRAV DIASSYIICK EAGALITDEN GDELKFDLNA TDRLNIIVAN
SKEMLDIILD LL
//
