YIGL_ECO57
ID YIGL_ECO57 Reviewed; 266 AA.
AC Q8X8L6;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pyridoxal phosphate phosphatase YigL;
DE EC=3.1.3.74;
DE AltName: Full=PLP phosphatase;
DE AltName: Full=Sugar phosphatase;
DE EC=3.1.3.23;
GN Name=yigL; OrderedLocusNames=Z5347, ECs4756;
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: Catalyzes the dephosphorylation of pyridoxal-phosphate (PLP)
CC and sugar phosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sugar phosphate + H2O = sugar + phosphate.; EC=3.1.3.23;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Magnesium. Can also use other divalent metal cations as manganese,
CC cobalt or zinc. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG59022.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG59022.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB38179.1; -; Genomic_DNA.
DR PIR; B86070; B86070.
DR PIR; D91223; D91223.
DR RefSeq; NP_312783.1; NC_002695.1.
DR RefSeq; WP_000285328.1; NZ_SDVX01000004.1.
DR AlphaFoldDB; Q8X8L6; -.
DR SMR; Q8X8L6; -.
DR STRING; 155864.EDL933_5148; -.
DR EnsemblBacteria; AAG59022; AAG59022; Z5347.
DR EnsemblBacteria; BAB38179; BAB38179; ECs_4756.
DR GeneID; 915148; -.
DR KEGG; ece:Z5347; -.
DR KEGG; ecs:ECs_4756; -.
DR PATRIC; fig|386585.9.peg.4965; -.
DR eggNOG; COG0561; Bacteria.
DR HOGENOM; CLU_044146_5_2_6; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
DR GO; GO:0050308; F:sugar-phosphatase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR000150; Cof.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR PROSITE; PS01228; COF_1; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..266
FT /note="Pyridoxal phosphate phosphatase YigL"
FT /id="PRO_0000054427"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 42..43
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 29704 MW; ECC345719C8B4CB5 CRC64;
MYQVVASDLD GTLLSPDHTL SPYAKEPLKL LTARGINFVF ATGRHHVDVG QIRDNLEIKS
YMITSNGARV HDLDGNLIFA HNLDRDIASD LFGVVNDNPD IITNVYRDDE WFMNRHRPEE
MRFFKEAVFK YALYEPGLLE PEGVSKVFFT CDSHEQLLPL EQAINARWGD RVNVSFSTLT
CLEVMAGGVS KGHALEAVAK KLGYSLKDCI AFGDGMNDAE MLSMAGKGCI MGSAHQRLKD
LHPELEVIGT NADDAVPHYL RKLYLS
