YAEI_ECOLI
ID YAEI_ECOLI Reviewed; 270 AA.
AC P37049; P75666; Q8KJP9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Phosphodiesterase YaeI;
DE EC=3.1.4.-;
GN Name=yaeI; OrderedLocusNames=b0164, JW5014;
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=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 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).
CC -!- FUNCTION: Shows phosphodiesterase activity, hydrolyzing phosphodiester
CC bond in the artificial chromogenic substrate bis-p-nitrophenyl
CC phosphate (bis-pNPP). {ECO:0000269|PubMed:15808744}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
CC {ECO:0000305}.
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DR EMBL; U70214; AAB08594.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73275.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96741.2; -; Genomic_DNA.
DR PIR; D64740; D64740.
DR RefSeq; NP_414706.2; NC_000913.3.
DR RefSeq; WP_000625631.1; NZ_SSZK01000004.1.
DR AlphaFoldDB; P37049; -.
DR SMR; P37049; -.
DR BioGRID; 4260646; 8.
DR STRING; 511145.b0164; -.
DR PaxDb; P37049; -.
DR PRIDE; P37049; -.
DR EnsemblBacteria; AAC73275; AAC73275; b0164.
DR EnsemblBacteria; BAB96741; BAB96741; BAB96741.
DR GeneID; 945002; -.
DR KEGG; ecj:JW5014; -.
DR KEGG; eco:b0164; -.
DR PATRIC; fig|511145.12.peg.170; -.
DR EchoBASE; EB2241; -.
DR eggNOG; COG1408; Bacteria.
DR HOGENOM; CLU_025443_3_2_6; -.
DR InParanoid; P37049; -.
DR OMA; PEYVYGE; -.
DR PhylomeDB; P37049; -.
DR BioCyc; EcoCyc:EG12337-MON; -.
DR BRENDA; 3.1.4.1; 2026.
DR PRO; PR:P37049; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:EcoCyc.
DR GO; GO:0008758; F:UDP-2,3-diacylglucosamine hydrolase activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..270
FT /note="Phosphodiesterase YaeI"
FT /id="PRO_0000172849"
FT BINDING 56
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 29863 MW; 6A075D0C09E5CAE7 CRC64;
MISRRRFLQA TAATIATSSG FGYMHYCEPG WFELIRHRLA FFKDNAAPFK ILFLADLHYS
RFVPLSLISD AIALGIEQKP DLILLGGDYV LFDMSLNFSA FSDVLSPLAE CAPTFACFGN
HDRPVGTEKN HLIGETLKSA GITVLFNQAT VIATPNRQFE LVGTGDLWAG QCKPPPASEA
NLPRLVLAHN PDSKEVMRDE PWDLMLCGHT HGGQLRVPLV GEPFAPVEDK RYVAGLNAFG
ERHIYTTRGV GSLYGLRLNC RPEVTMLELV
