BSUHB_ARCFU
ID BSUHB_ARCFU Reviewed; 252 AA.
AC O30298;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase;
DE Short=FBPase/IMPase;
DE EC=3.1.3.11 {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
DE EC=3.1.3.25 {ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
DE AltName: Full=Inositol-1-phosphatase;
DE Short=I-1-Pase;
GN Name=suhB; OrderedLocusNames=AF_2372;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION AS IMPASE, AND CATALYTIC ACTIVITY.
RX PubMed=10747806; DOI=10.1021/bi992424f;
RA Chen L., Roberts M.F.;
RT "Overexpression, purification, and analysis of complementation behavior of
RT E. coli SuhB protein: comparison with bacterial and archaeal inositol
RT monophosphatases.";
RL Biochemistry 39:4145-4153(2000).
RN [3]
RP FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
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 (1.8 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP I-1-P; FBP; F-6-P AND METAL IONS, FUNCTION AS BOTH FBPASE AND IMPASE,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, ACTIVITY
RP REGULATION, AND COFACTOR.
RX PubMed=11940584; DOI=10.1074/jbc.m201042200;
RA Stieglitz K.A., Johnson K.A., Yang H., Roberts M.F., Seaton B.A.,
RA Head J.F., Stec B.;
RT "Crystal structure of a dual activity IMPase/FBPase (AF2372) from
RT Archaeoglobus fulgidus. The story of a mobile loop.";
RL J. Biol. Chem. 277:22863-22874(2002).
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, inositol-2-phosphate, beta-glycerol phosphate,
CC and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate
CC and fructose-6-phosphate. May be involved in the biosynthesis of a
CC unique osmolyte, di-myo-inositol 1,1-phosphate.
CC {ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:11062561,
CC ECO:0000269|PubMed:11940584}.
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, ECO:0000269|PubMed:11940584};
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:10747806, ECO:0000269|PubMed:11062561,
CC ECO:0000269|PubMed:11940584};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11940584};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11940584};
CC Note=Magnesium. Can also use manganese. {ECO:0000269|PubMed:11940584};
CC -!- ACTIVITY REGULATION: Both FBPase and IMPase activities are inhibited by
CC Ca(2+). In contrast to mammalian I-1-P phosphatases, is only very
CC weakly inhibited by Li(+) (with an IC(50) of about 290 mM).
CC {ECO:0000269|PubMed:11940584}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for inositol-1-phosphate (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
CC KM=0.08 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
CC Vmax=3.27 umol/min/mg enzyme with L-inositol-1-phosphate as substrate
CC (at 80 degrees Celsius, pH 8, in the presence of Mg(2+))
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
CC Vmax=2.20 umol/min/mg enzyme with L-inositol-1-phosphate as substrate
CC (at 80 degrees Celsius, pH 8, in the presence of Mn(2+))
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
CC Vmax=1.52 umol/min/mg enzyme with D-fructose 1,6-bisphosphate as
CC substrate (at 80 degrees Celsius, pH 8, in the presence of Mg(2+))
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
CC Vmax=1.92 umol/min/mg enzyme with D-fructose 1,6-bisphosphate as
CC substrate (at 80 degrees Celsius, pH 8, in the presence of Mn(2+))
CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
CC Note=kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius)
CC and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius).
CC {ECO:0000269|PubMed:11062561};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11062561}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91288.1; -; Genomic_DNA.
DR PIR; D69546; D69546.
DR RefSeq; WP_010879859.1; NC_000917.1.
DR PDB; 1LBV; X-ray; 1.80 A; A/B=1-252.
DR PDB; 1LBW; X-ray; 2.00 A; A/B=1-252.
DR PDB; 1LBX; X-ray; 2.40 A; A/B=1-252.
DR PDB; 1LBY; X-ray; 2.25 A; A/B=1-252.
DR PDB; 1LBZ; X-ray; 2.20 A; A/B=1-252.
DR PDB; 6B5Z; X-ray; 2.30 A; A/B=1-252.
DR PDB; 6B60; X-ray; 2.70 A; A/B=1-252.
DR PDB; 6B61; X-ray; 2.70 A; A/B=1-252.
DR PDB; 6B62; X-ray; 2.00 A; A/B=1-252.
DR PDB; 6B63; X-ray; 2.70 A; A/B=1-252.
DR PDB; 6B64; X-ray; 2.60 A; A/B=1-252.
DR PDB; 6B65; X-ray; 2.70 A; A/B=1-252.
DR PDB; 6B66; X-ray; 2.50 A; A/B=1-252.
DR PDBsum; 1LBV; -.
DR PDBsum; 1LBW; -.
DR PDBsum; 1LBX; -.
DR PDBsum; 1LBY; -.
DR PDBsum; 1LBZ; -.
DR PDBsum; 6B5Z; -.
DR PDBsum; 6B60; -.
DR PDBsum; 6B61; -.
DR PDBsum; 6B62; -.
DR PDBsum; 6B63; -.
DR PDBsum; 6B64; -.
DR PDBsum; 6B65; -.
DR PDBsum; 6B66; -.
DR AlphaFoldDB; O30298; -.
DR SMR; O30298; -.
DR STRING; 224325.AF_2372; -.
DR EnsemblBacteria; AAB91288; AAB91288; AF_2372.
DR GeneID; 24796117; -.
DR KEGG; afu:AF_2372; -.
DR eggNOG; arCOG01349; Archaea.
DR HOGENOM; CLU_044118_5_0_2; -.
DR OMA; RWGDERY; -.
DR OrthoDB; 99063at2157; -.
DR PhylomeDB; O30298; -.
DR BRENDA; 3.1.3.108; 414.
DR BRENDA; 3.1.3.11; 414.
DR BRENDA; 3.1.3.25; 414.
DR SABIO-RK; O30298; -.
DR EvolutionaryTrace; O30298; -.
DR Proteomes; UP000002199; 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:UniProtKB-EC.
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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
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; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..252
FT /note="Fructose-1,6-bisphosphatase/inositol-1-
FT monophosphatase"
FT /id="PRO_0000142579"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 85..87
FT /ligand="substrate"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 167
FT /ligand="substrate"
FT BINDING 172
FT /ligand="substrate"
FT BINDING 191
FT /ligand="substrate"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1LBV"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:1LBV"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1LBV"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1LBV"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1LBV"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:1LBV"
SQ SEQUENCE 252 AA; 27967 MW; EF48983721AEA687 CRC64;
MDERDALRIS REIAGEVRKA IASMPLRERV KDVGMGKDGT PTKAADRVAE DAALEILRKE
RVTVVTEESG VLGEGDVFVA LDPLDGTFNA TRGIPVYSVS LCFSYSDKLK DAFFGYVYNL
ATGDEYYADS SGAYRNGERI EVSDAEELYC NAIIYYPDRK FPFKRMRIFG SAATELCFFA
DGSFDCFLDI RPGKMLRIYD AAAGVFIAEK AGGKVTELDG ESLGNKKFDM QERLNIVAAN
EKLHPKLLEL IK
