ID   Q12XM3_METBU            Unreviewed;       266 AA.
AC   Q12XM3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   04-NOV-2026, entry version 102.
DE   RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093};
DE            EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
GN   OrderedLocusNames=Mbur_0852 {ECO:0000313|EMBL:ABE51803.1};
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564 {ECO:0000313|EMBL:ABE51803.1, ECO:0000313|Proteomes:UP000001979};
RN   [1] {ECO:0000313|Proteomes:UP000001979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M
RC   {ECO:0000313|Proteomes:UP000001979};
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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:0000256|ARBA:ARBA00001273};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR600760-2};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC       class 4 family. {ECO:0000256|ARBA:ARBA00038103}.
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DR   EMBL; CP000300; ABE51803.1; -; Genomic_DNA.
DR   RefSeq; WP_011498956.1; NC_007955.1.
DR   AlphaFoldDB; Q12XM3; -.
DR   STRING; 259564.Mbur_0852; -.
DR   GeneID; 3996757; -.
DR   KEGG; mbu:Mbur_0852; -.
DR   HOGENOM; CLU_044118_5_0_2; -.
DR   OMA; AALEMCM; -.
DR   OrthoDB; 58111at2157; -.
DR   Proteomes; UP000001979; 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; IEA:TreeGrafter.
DR   GO; GO:0006020; P:inositol metabolic process; IEA:TreeGrafter.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:TreeGrafter.
DR   CDD; cd01515; Arch_FBPase_1; 1.
DR   FunFam; 3.30.540.10:FF:000027; Fructose-1,6-bisphosphatase/inositol-1-monophosphatase; 1.
DR   FunFam; 3.40.190.80:FF:000020; Fructose-1,6-bisphosphatase/inositol-1-monophosphatase; 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; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   NCBIfam; NF009321; PRK12676.1; 1.
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; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABE51803.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR600760-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR600760-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001979}.
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600760-2"
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600760-2"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600760-2"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600760-2"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600760-2"
SQ   SEQUENCE   266 AA;  28933 MW;  BDB14DC146289A18 CRC64;
     MSVSQQILEF CDLLAESASN AISDIVGTEE AFRTVYVGAD GTDTKLIDDV SEKAIIEILK
     ADGRSIRLLS EELGEVVFGD DPEFTIILDP IDGTYNVAND IPFYGISIAI GTPDLSSTYF
     GYVRNLANGD TFYAESGKGA YFNDKRISHS KCSSLNDFCV SLYGYRKNVE RTVDLCKNVR
     RIRIFGSVSL ELCYVASGRL DAFVDVRGSL RLVDVAAGKL IIEESGGIVT DGDGNTLKLK
     DSVINPVYMV ASNGCAHSDI LKLVMR
//