HXPA_ECOLI
ID HXPA_ECOLI Reviewed; 216 AA.
AC P77625;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Hexitol phosphatase A {ECO:0000303|PubMed:27941785};
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=hxpA {ECO:0000303|PubMed:27941785};
GN Synonyms=yfbT {ECO:0000312|EMBL:AAC75353.2};
GN OrderedLocusNames=b2293, JW5376;
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=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP FUNCTION AS A PHOSPHATASE.
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 [6]
RP FUNCTION AS A SUGAR-PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND COFACTOR.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Sugar-phosphate phosphohydrolase that appears to contribute
CC to butanol tolerance (PubMed:27941785). Catalyzes the dephosphorylation
CC of D-mannitol 1-phosphate and D-sorbitol 6-phosphate (PubMed:27941785).
CC Is also able to dephosphorylate other sugar phosphates in vitro
CC including ribose-5-phosphate (Rib5P), 2-deoxyribose-5-phosphate,
CC fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), and
CC glucose-6-phosphate (Glu6P) (PubMed:16990279). Selectively hydrolyzes
CC beta-D-glucose-1-phosphate (bGlu1P) and has no activity with the alpha
CC form (PubMed:16990279). {ECO:0000269|PubMed:15808744,
CC ECO:0000269|PubMed:16990279, 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=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 Note=Requires the presence of a divalent metal cation for activity. Can
CC use magnesium, manganese or cobalt. {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for fructose-1-P (with magnesium ions as cofactor and at pH
CC 9) {ECO:0000269|PubMed:16990279};
CC KM=1.3 mM for fructose-6-P (with magnesium ions as cofactor and at pH
CC 9) {ECO:0000269|PubMed:16990279};
CC KM=1.8 mM for glucose-6-P (with cobalt ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=2.2 mM for ribose-5-P (with magnesium ions as cofactor and at pH
CC 9) {ECO:0000269|PubMed:16990279};
CC KM=7.0 mM for beta-D-glucose-1-P (with manganese ions as cofactor and
CC at pH 9) {ECO:0000269|PubMed:16990279};
CC Note=kcat is 3.7 sec(-1) with fructose-1-P as substrate. kcat is 2.7
CC sec(-1) with ribose-5-P as substrate. kcat is 13 sec(-1) with
CC glucose-6-P as substrate. kcat is 3.1 sec(-1) with fructose-6-P as
CC substrate. kcat is 7.5 sec(-1) with beta-D-glucose-1-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 show a reduced growth
CC rate at high butanol concentrations compared to wild-type. They also
CC show a consistent change in the level of mannitol, D-sorbitol,
CC galactitol, L-tyrosine, 3-amino-3-(4-hydroxyphenyl)propanoate and N-
CC hydroxy-L-phenylalanine. {ECO:0000269|PubMed:27941785}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; U00096; AAC75353.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16129.2; -; Genomic_DNA.
DR PIR; C65001; C65001.
DR RefSeq; NP_416796.2; NC_000913.3.
DR RefSeq; WP_001203392.1; NZ_LN832404.1.
DR AlphaFoldDB; P77625; -.
DR SMR; P77625; -.
DR BioGRID; 4262967; 8.
DR BioGRID; 851118; 1.
DR DIP; DIP-11972N; -.
DR IntAct; P77625; 2.
DR STRING; 511145.b2293; -.
DR jPOST; P77625; -.
DR PaxDb; P77625; -.
DR PRIDE; P77625; -.
DR EnsemblBacteria; AAC75353; AAC75353; b2293.
DR EnsemblBacteria; BAA16129; BAA16129; BAA16129.
DR GeneID; 946777; -.
DR KEGG; ecj:JW5376; -.
DR KEGG; eco:b2293; -.
DR PATRIC; fig|511145.12.peg.2387; -.
DR EchoBASE; EB3857; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_4_6; -.
DR InParanoid; P77625; -.
DR OMA; VVERSWC; -.
DR PhylomeDB; P77625; -.
DR BioCyc; EcoCyc:G7187-MON; -.
DR BioCyc; MetaCyc:G7187-MON; -.
DR PRO; PR:P77625; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0050084; F:mannitol-1-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0050286; F:sorbitol-6-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA: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; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cobalt; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..216
FT /note="Hexitol phosphatase A"
FT /id="PRO_0000108059"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 11
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 106..107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
SQ SEQUENCE 216 AA; 23008 MW; C687DF877E2706EF CRC64;
MRCKGFLFDL DGTLVDSLPA VERAWSNWAR RHGLAPEEVL AFIHGKQAIT SLRHFMAGKS
EADIAAEFTR LEHIEATETE GITALPGAIA LLSHLNKAGI PWAIVTSGSM PVARARHKIA
GLPAPEVFVT AERVKRGKPE PDAYLLGAQL LGLAPQECVV VEDAPAGVLS GLAAGCHVIA
VNAPADTPRL NEVDLVLHSL EQITVTKQPN GDVIIQ
