HXPB_ECO57
ID HXPB_ECO57 Reviewed; 222 AA.
AC Q7ADF8; Q8XEJ5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hexitol phosphatase B {ECO:0000250|UniProtKB:P77247};
DE AltName: Full=2-deoxyglucose-6-phosphate phosphatase {ECO:0000250|UniProtKB:P77247};
DE EC=3.1.3.68 {ECO:0000250|UniProtKB:P77247};
DE AltName: Full=Mannitol-1-phosphatase {ECO:0000250|UniProtKB:P77247};
DE EC=3.1.3.22 {ECO:0000250|UniProtKB:P77247};
DE AltName: Full=Sorbitol-6-phosphatase {ECO:0000250|UniProtKB:P77247};
DE EC=3.1.3.50 {ECO:0000250|UniProtKB:P77247};
DE AltName: Full=Sugar-phosphatase {ECO:0000250|UniProtKB:P77247};
DE EC=3.1.3.23 {ECO:0000250|UniProtKB:P77247};
GN Name=hxpB {ECO:0000250|UniProtKB:P77247}; Synonyms=yniC;
GN OrderedLocusNames=Z2756, ECs2433;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Sugar-phosphate phosphohydrolase that catalyzes the
CC dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate.
CC Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate
CC (2dGlu6P); this is a biologically important activity in vivo since it
CC contributes to the elimination of this toxic compound and plays an
CC important role in the resistance of E.coli to 2-deoxyglucose.
CC {ECO:0000250|UniProtKB:P77247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sugar phosphate + H2O = sugar + phosphate.; EC=3.1.3.23;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-D-glucose 6-phosphate + H2O = 2-deoxy-D-glucose +
CC phosphate; Xref=Rhea:RHEA:22236, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84755, ChEBI:CHEBI:84760; EC=3.1.3.68;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + H2O = D-mannitol + phosphate;
CC Xref=Rhea:RHEA:19537, ChEBI:CHEBI:15377, ChEBI:CHEBI:16899,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61381; EC=3.1.3.22;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol 6-phosphate + H2O = D-sorbitol + phosphate;
CC Xref=Rhea:RHEA:24580, ChEBI:CHEBI:15377, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60084; EC=3.1.3.50;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P77247};
CC Note=Requires the presence of a divalent metal cation for activity. Can
CC use zinc, manganese, cobalt or magnesium.
CC {ECO:0000250|UniProtKB:P77247};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; AE005174; AAG56713.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35856.1; -; Genomic_DNA.
DR PIR; A98933; A98933.
DR PIR; E85781; E85781.
DR RefSeq; NP_310460.1; NC_002695.1.
DR RefSeq; WP_000106834.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; Q7ADF8; -.
DR SMR; Q7ADF8; -.
DR STRING; 155864.EDL933_2686; -.
DR DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR EnsemblBacteria; AAG56713; AAG56713; Z2756.
DR EnsemblBacteria; BAB35856; BAB35856; ECs_2433.
DR GeneID; 66674379; -.
DR GeneID; 912766; -.
DR KEGG; ece:Z2756; -.
DR KEGG; ecs:ECs_2433; -.
DR PATRIC; fig|386585.9.peg.2547; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_1_6; -.
DR OMA; LWDNDGL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0003850; F:2-deoxyglucose-6-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0050084; F:mannitol-1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0050286; F:sorbitol-6-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050308; F:sugar-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cobalt; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..222
FT /note="Hexitol phosphatase B"
FT /id="PRO_0000108062"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT ACT_SITE 15
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT BINDING 13..15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 13
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT CONFLICT 205
FT /note="A -> S (in Ref. 1; AAG56713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 24329 MW; 7B937F2A331476A7 CRC64;
MSTPRQILAA IFDMDGLLID SEPLWDRAEL DVMASLGVDI SRRNELPDTL GLRIDMVVDL
WYARQPWNGP SRQEVVERVI ARAISLVEET RPLLPGVREA VALCKEQGLL VGLASASPLH
MLEKVLTMFD LRDSFDALAS AEKLPYSKPH PQVYLDCAAK LGVDPLTCVA LEDSVNGMIA
SKAARMRSIV VPAPEAQNDP RFVLANVKLS SLTELTAKDL LG
