F16PA_METI4
ID F16PA_METI4 Reviewed; 356 AA.
AC B3DWS5; A9QPD3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE Short=FBPase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=Minf_1684;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum.
OX NCBI_TaxID=481448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4;
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-356.
RX PubMed=18004300; DOI=10.1038/nature06411;
RA Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S.,
RA Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., Crowe M.A.,
RA Weatherby T.M., Bodelier P.L.E., Liesack W., Feng L., Wang L., Alam M.;
RT "Methane oxidation by an extremely acidophilic bacterium of the phylum
RT Verrucomicrobia.";
RL Nature 450:879-882(2007).
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:0000255|HAMAP-Rule:MF_01855};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01855};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01855}.
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DR EMBL; CP000975; ACD83738.1; -; Genomic_DNA.
DR EMBL; EU223849; ABX56591.1; -; Genomic_DNA.
DR RefSeq; WP_012464020.1; NC_010794.1.
DR AlphaFoldDB; B3DWS5; -.
DR SMR; B3DWS5; -.
DR STRING; 481448.Minf_1684; -.
DR EnsemblBacteria; ACD83738; ACD83738; Minf_1684.
DR KEGG; min:Minf_1684; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_0_0_0; -.
DR OMA; YIPENCP; -.
DR OrthoDB; 945770at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009149; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..356
FT /note="Fructose-1,6-bisphosphatase class 1"
FT /id="PRO_0000364595"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 116..119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ SEQUENCE 356 AA; 40216 MW; F90B92F1888D0836 CRC64;
MSYHRMTLSK FLLEQRKKGV IDPDLGSLIN DIESACKYVA AAVSKGKLIS QEVNVTINVQ
GEEQKPLDVI ANEIFLKICE QGDQLQGMVS EEMESPYIIP PEHRRGKYLL IYDPLDGSSN
LDVNLTVGSI FSVLKAPESG EPLEEKHFLR PGREQLAAGF TLYGPSVMFI LTLGNGVHGF
TLDREVGIFT LTHPDMRITP STKEFAINAS NERFWEPPVR RYVEECIKGK TGPRGKDFNM
RWIASMVAEV YRILIRGGLF MYPRDTKDLS KPGRLRLLYE ANPMGFIVEQ AGGMISTGRE
SILDIVPRSL HQRIAVILGS KEEVELLNRY HNDYDSGKQE EFESPLFSTR SLFRNP
