YIGL_ECOLI
ID YIGL_ECOLI Reviewed; 266 AA.
AC P27848; P76763; Q2M8D1; Q6BEY9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 4.
DT 03-AUG-2022, entry version 153.
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=b3826, JW5854;
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=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
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 SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83.
RC STRAIN=K12 / KL16-99;
RX PubMed=3908445; DOI=10.1093/oxfordjournals.jbchem.a135347;
RA Kobayashi T., Kudo I., Karasawa K., Mizushima H., Inoue K., Nojima S.;
RT "Nucleotide sequence of the pldB gene and characteristics of deduced amino
RT acid sequence of lysophospholipase L2 in Escherichia coli.";
RL J. Biochem. 98:1017-1025(1985).
RN [6]
RP FUNCTION AS A 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).
CC -!- FUNCTION: Catalyzes Strongly the dephosphorylation of pyridoxal-
CC phosphate (PLP) and moderately the dephosphorylation of 2-deoxyglucose
CC 6-phosphate (2bGLU6P) and beta-glucose 6-phosphate (bGlu6P). Also
CC hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary
CC substrates. {ECO:0000269|PubMed:16990279}.
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 Evidence={ECO:0000269|PubMed:16990279};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sugar phosphate + H2O = sugar + phosphate.; EC=3.1.3.23;
CC Evidence={ECO:0000269|PubMed:16990279};
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 as manganese,
CC cobalt or zinc. {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for PLP (in the presence of magnesium ion as cofactor and
CC at pH 9) {ECO:0000269|PubMed:16990279};
CC KM=5.9 mM for bGlu6P (in the presence of magnesium ion as cofactor
CC and at pH 9) {ECO:0000269|PubMed:16990279};
CC KM=7.5 mM for 2bGLU6P (in the presence of magnesium ion as cofactor
CC and at pH 9) {ECO:0000269|PubMed:16990279};
CC pH dependence:
CC Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67622.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M87049; AAA67622.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48225.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77475.1; -; Genomic_DNA.
DR EMBL; X03155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_000285362.1; NZ_SSZK01000046.1.
DR RefSeq; YP_026267.1; NC_000913.3.
DR AlphaFoldDB; P27848; -.
DR SMR; P27848; -.
DR BioGRID; 4259609; 11.
DR BioGRID; 853515; 2.
DR IntAct; P27848; 2.
DR STRING; 511145.b3826; -.
DR jPOST; P27848; -.
DR PaxDb; P27848; -.
DR PRIDE; P27848; -.
DR DNASU; 2847768; -.
DR EnsemblBacteria; AAT48225; AAT48225; b3826.
DR EnsemblBacteria; BAE77475; BAE77475; BAE77475.
DR GeneID; 2847768; -.
DR KEGG; ecj:JW5854; -.
DR KEGG; eco:b3826; -.
DR PATRIC; fig|511145.12.peg.3942; -.
DR EchoBASE; EB1438; -.
DR eggNOG; COG0561; Bacteria.
DR HOGENOM; CLU_044146_5_2_6; -.
DR InParanoid; P27848; -.
DR OMA; CCAERGI; -.
DR PhylomeDB; P27848; -.
DR BioCyc; EcoCyc:EG11470-MON; -.
DR BioCyc; MetaCyc:EG11470-MON; -.
DR PRO; PR:P27848; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki.
DR GO; GO:0016791; F:phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..266
FT /note="Pyridoxal phosphate phosphatase YigL"
FT /id="PRO_0000054426"
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; 29708 MW; 7C9AFE9CF13D8B2B CRC64;
MYQVVASDLD GTLLSPDHTL SPYAKETLKL LTARGINFVF ATGRHHVDVG QIRDNLEIKS
YMITSNGARV HDLDGNLIFA HNLDRDIASD LFGVVNDNPD IITNVYRDDE WFMNRHRPEE
MRFFKEAVFQ YALYEPGLLE PEGVSKVFFT CDSHEQLLPL EQAINARWGD RVNVSFSTLT
CLEVMAGGVS KGHALEAVAK KLGYSLKDCI AFGDGMNDAE MLSMAGKGCI MGSAHQRLKD
LHPELEVIGT NADDAVPHYL RKLYLS
