YIHX_ECOLI
ID YIHX_ECOLI Reviewed; 199 AA.
AC P0A8Y3; P32145; Q2M8I2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alpha-D-glucose 1-phosphate phosphatase YihX;
DE Short=Alpha-D-glucose-1-P phosphatase;
DE EC=3.1.3.10 {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:25484615};
DE AltName: Full=Alpha-D-glucose-1-phosphatase;
DE AltName: Full=Haloacid dehalogenase-like phosphatase 4 {ECO:0000303|PubMed:25484615};
DE Short=HAD4 {ECO:0000303|PubMed:16990279, ECO:0000303|PubMed:25484615};
GN Name=yihX; OrderedLocusNames=b3885, JW5566;
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 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND BIOTECHNOLOGY.
RX PubMed=25484615; DOI=10.1016/j.molcatb.2014.09.004;
RA Pfeiffer M., Wildberger P., Nidetzky B.;
RT "Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia
RT coli is a specific alpha-d-glucose 1-phosphate hydrolase useful for
RT substrate-selective sugar phosphate transformations.";
RL J. Mol. Catal., B Enzym. 110:39-46(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RG Midwest center for structural genomics (MCSG);
RT "The 2.0a crystal structure of the putative phosphatase from Escherichia
RT coli.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the dephosphorylation of alpha-D-glucose 1-
CC phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates
CC (PubMed:16990279) (PubMed:25484615). Has no activity with the beta form
CC of Glc1P. In addition, YihX has significant phosphatase activity
CC against pyridoxal phosphate (PLP) and low beta-phosphoglucomutase
CC activity (PubMed:16990279). {ECO:0000269|PubMed:16990279,
CC ECO:0000269|PubMed:25484615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate;
CC Xref=Rhea:RHEA:19933, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=3.1.3.10;
CC Evidence={ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:25484615};
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=Magnesium. Can also use other divalent metal cations such as
CC manganese, cobalt or zinc. {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.028 mM for imido-di-P (with magnesium ions as cofactor and at pH
CC 9) {ECO:0000269|PubMed:16990279};
CC KM=0.24 mM for alpha-D-glucose-1-phosphate (with magnesium ions as
CC cofactor and at pH 9) {ECO:0000269|PubMed:16990279};
CC KM=1.6 mM for alpha-fructose-1-phosphate (with manganese ions as
CC cofactor and at pH 9) {ECO:0000269|PubMed:16990279};
CC KM=3.6 mM for acetyl-phosphate (with magnesium ions as cofactor and
CC at pH 9) {ECO:0000269|PubMed:16990279};
CC Note=kcat is 10.2 sec(-1) with alpha-Glc-1-P as substrate. kcat is
CC 1.26 sec(-1) with alpha-Man-1-P as substrate. kcat is 0.98 sec(-1)
CC with alpha-Gal-1-P as substrate. kcat is 0.09 sec(-1) with Glc-6-P as
CC substrate (at pH 7.0 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:25484615};
CC pH dependence:
CC Optimum pH is 5.0-7.0. {ECO:0000269|PubMed:16990279,
CC ECO:0000269|PubMed:25484615};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:25484615};
CC -!- BIOTECHNOLOGY: Is proposed to be a useful catalyst for hydrolytic
CC transformation (e.g. removal) of alpha-Glc-1-P from complex substrate
CC solutions containing multiple sugar phosphates.
CC {ECO:0000305|PubMed:25484615}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. YihX family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03018.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L19201; AAB03018.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAD13447.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77424.1; -; Genomic_DNA.
DR PIR; S40829; S40829.
DR RefSeq; NP_418321.4; NC_000913.3.
DR RefSeq; WP_001295269.1; NZ_STEB01000017.1.
DR PDB; 2B0C; X-ray; 2.00 A; A=1-199.
DR PDBsum; 2B0C; -.
DR AlphaFoldDB; P0A8Y3; -.
DR SMR; P0A8Y3; -.
DR BioGRID; 4260964; 8.
DR DIP; DIP-47896N; -.
DR STRING; 511145.b3885; -.
DR jPOST; P0A8Y3; -.
DR PaxDb; P0A8Y3; -.
DR PRIDE; P0A8Y3; -.
DR EnsemblBacteria; AAD13447; AAD13447; b3885.
DR EnsemblBacteria; BAE77424; BAE77424; BAE77424.
DR GeneID; 66672209; -.
DR GeneID; 948380; -.
DR KEGG; ecj:JW5566; -.
DR KEGG; eco:b3885; -.
DR PATRIC; fig|1411691.4.peg.2826; -.
DR EchoBASE; EB1796; -.
DR eggNOG; COG1011; Bacteria.
DR HOGENOM; CLU_045011_9_5_6; -.
DR InParanoid; P0A8Y3; -.
DR OMA; IDIDFNR; -.
DR PhylomeDB; P0A8Y3; -.
DR BioCyc; EcoCyc:EG11850-MON; -.
DR BioCyc; MetaCyc:EG11850-MON; -.
DR EvolutionaryTrace; P0A8Y3; -.
DR PRO; PR:P0A8Y3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008877; F:glucose-1-phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
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; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..199
FT /note="Alpha-D-glucose 1-phosphate phosphatase YihX"
FT /id="PRO_0000066265"
FT ACT_SITE 6
FT /note="Nucleophile"
FT BINDING 6..8
FT /ligand="substrate"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="substrate"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.7"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2B0C"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2B0C"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:2B0C"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2B0C"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2B0C"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2B0C"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:2B0C"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2B0C"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2B0C"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:2B0C"
SQ SEQUENCE 199 AA; 22732 MW; 9451EA8917DFC0D2 CRC64;
MLYIFDLGNV IVDIDFNRVL GAWSDLTRIP LASLKKSFHM GEAFHQHERG EISDEAFAEA
LCHEMALPLS YEQFSHGWQA VFVALRPEVI AIMHKLREQG HRVVVLSNTN RLHTTFWPEE
YPEIRDAADH IYLSQDLGMR KPEARIYQHV LQAEGFSPSD TVFFDDNADN IEGANQLGIT
SILVKDKTTI PDYFAKVLC
