HXPB_ECOLI
ID HXPB_ECOLI Reviewed; 222 AA.
AC P77247; P78167;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Hexitol phosphatase B {ECO:0000303|PubMed:27941785};
DE AltName: Full=2-deoxyglucose-6-phosphate phosphatase {ECO:0000305|PubMed:16990279};
DE EC=3.1.3.68 {ECO:0000269|PubMed:16990279};
DE AltName: Full=Mannitol-1-phosphatase {ECO:0000305|PubMed:27941785};
DE EC=3.1.3.22 {ECO:0000269|PubMed:27941785};
DE AltName: Full=Sorbitol-6-phosphatase {ECO:0000305|PubMed:27941785};
DE EC=3.1.3.50 {ECO:0000269|PubMed:27941785};
DE AltName: Full=Sugar-phosphatase {ECO:0000305|PubMed:16990279};
DE EC=3.1.3.23 {ECO:0000269|PubMed:16990279};
GN Name=hxpB {ECO:0000303|PubMed:27941785};
GN Synonyms=yniC {ECO:0000312|EMBL:AAC74797.1};
GN OrderedLocusNames=b1727, JW1716;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [5]
RP FUNCTION AS A SUGAR-PHOSPHATASE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-13,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND COFACTOR.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia coli
RT haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(2006).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=27941785; DOI=10.1038/nmeth.4103;
RA Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
RT "Nontargeted in vitro metabolomics for high-throughput identification of
RT novel enzymes in Escherichia coli.";
RL Nat. Methods 14:187-194(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH A SUBSTRATE ANALOG
RP AND CALCIUM IONS.
RA Kim Y., Joachimiak A., Evdokimova E., Savchenko A., Edwards A.M.;
RT "Crystal structure of putative phosphatase YniC from Escherichia coli
RT K12.";
RL Submitted (AUG-2004) to the PDB data bank.
CC -!- FUNCTION: Sugar-phosphate phosphohydrolase that catalyzes the
CC dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate
CC (PubMed:27941785). Also catalyzes the dephosphorylation of 2-
CC deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important
CC activity in vivo since it contributes to the elimination of this toxic
CC compound and plays an important role in the resistance of E.coli to 2-
CC deoxyglucose (PubMed:16990279). To a lesser extent, is also able to
CC dephosphorylate mannose 6-phosphate (Man6P), erythrose-4-phosphate, 2-
CC deoxyribose-5-phosphate (2dRib5P), ribose-5-phosphate (Rib5P) and
CC glucose-6-phosphate (Glu6P) in vitro (PubMed:16990279).
CC {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279,
CC ECO:0000269|PubMed:27941785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sugar phosphate + H2O = sugar + phosphate.; EC=3.1.3.23;
CC Evidence={ECO:0000269|PubMed:16990279};
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:0000269|PubMed:16990279};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Note=Requires the presence of a divalent metal cation for activity. Can
CC use zinc, manganese, cobalt or magnesium.
CC {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for 2-deoxyglucose-6-P (with manganese ions as cofactor
CC and at pH 9) {ECO:0000269|PubMed:16990279};
CC KM=2.5 mM for 2-deoxyribose-5-P (with zinc ions as cofactor and at pH
CC 9) {ECO:0000269|PubMed:16990279};
CC KM=2.6 mM for ribose-5-P (with zinc ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=3.6 mM for glucose-6-P (with zinc ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=4.7 mM for mannose-6-P (with zinc ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC Note=kcat is 33 sec(-1) with 2-deoxyglucose-6-P as substrate. kcat is
CC 11 sec(-1) with mannose-6-P as substrate. kcat is 9.4 sec(-1) with 2-
CC deoxyribose-5-P as substrate. kcat is 2.8 sec(-1) with ribose-5-P as
CC substrate. kcat is 25 sec(-1) with glucose-6-P as substrate.
CC {ECO:0000269|PubMed:16990279};
CC pH dependence:
CC Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are much more sensitive
CC to the presence of 2-deoxyglucose in the growth medium than wild-type.
CC {ECO:0000269|PubMed:16990279}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; U00096; AAC74797.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15508.1; -; Genomic_DNA.
DR PIR; G64931; G64931.
DR RefSeq; NP_416241.1; NC_000913.3.
DR RefSeq; WP_000106833.1; NZ_SSZK01000001.1.
DR PDB; 1TE2; X-ray; 1.76 A; A/B=1-222.
DR PDBsum; 1TE2; -.
DR AlphaFoldDB; P77247; -.
DR SMR; P77247; -.
DR BioGRID; 4263414; 9.
DR DIP; DIP-12777N; -.
DR IntAct; P77247; 8.
DR STRING; 511145.b1727; -.
DR SWISS-2DPAGE; P77247; -.
DR jPOST; P77247; -.
DR PaxDb; P77247; -.
DR PRIDE; P77247; -.
DR DNASU; 945632; -.
DR EnsemblBacteria; AAC74797; AAC74797; b1727.
DR EnsemblBacteria; BAA15508; BAA15508; BAA15508.
DR GeneID; 945632; -.
DR KEGG; ecj:JW1716; -.
DR KEGG; eco:b1727; -.
DR PATRIC; fig|1411691.4.peg.529; -.
DR EchoBASE; EB3744; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_1_6; -.
DR InParanoid; P77247; -.
DR OMA; LWDNDGL; -.
DR PhylomeDB; P77247; -.
DR BioCyc; EcoCyc:G6932-MON; -.
DR BioCyc; MetaCyc:G6932-MON; -.
DR EvolutionaryTrace; P77247; -.
DR PRO; PR:P77247; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003850; F:2-deoxyglucose-6-phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0050084; F:mannitol-1-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki.
DR GO; GO:0016791; F:phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0050286; F:sorbitol-6-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cobalt; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..222
FT /note="Hexitol phosphatase B"
FT /id="PRO_0000108061"
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:0000305|Ref.7"
FT BINDING 13
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.7"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.7"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 13
FT /note="D->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:16990279"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1TE2"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:1TE2"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:1TE2"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1TE2"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1TE2"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1TE2"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1TE2"
FT TURN 194..198
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:1TE2"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1TE2"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1TE2"
SQ SEQUENCE 222 AA; 24330 MW; 76FE1F2A331476A7 CRC64;
MSTPRQILAA IFDMDGLLID SEPLWDRAEL DVMASLGVDI SRRNELPDTL GLRIDMVVDL
WYARQPWNGP SRQEVVERVI ARAISLVEET RPLLPGVREA VALCKEQGLL VGLASASPLH
MLEKVLTMFD LRDSFDALAS AEKLPYSKPH PQVYLDCAAK LGVDPLTCVA LEDSVNGMIA
SKAARMRSIV VPAPEAQNDP RFVLADVKLS SLTELTAKDL LG
