YDEN_ECOLI
ID YDEN_ECOLI Reviewed; 560 AA.
AC P77318; P78159;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Uncharacterized sulfatase YdeN;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=ydeN; OrderedLocusNames=b1498, JW5243;
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=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {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; U00096; AAC74571.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15169.2; -; Genomic_DNA.
DR PIR; E64903; E64903.
DR RefSeq; NP_416015.2; NC_000913.3.
DR RefSeq; WP_001295684.1; NZ_STEB01000052.1.
DR AlphaFoldDB; P77318; -.
DR SMR; P77318; -.
DR BioGRID; 4260850; 26.
DR DIP; DIP-11682N; -.
DR IntAct; P77318; 1.
DR STRING; 511145.b1498; -.
DR jPOST; P77318; -.
DR PaxDb; P77318; -.
DR PRIDE; P77318; -.
DR EnsemblBacteria; AAC74571; AAC74571; b1498.
DR EnsemblBacteria; BAA15169; BAA15169; BAA15169.
DR GeneID; 66674649; -.
DR GeneID; 945957; -.
DR KEGG; ecj:JW5243; -.
DR KEGG; eco:b1498; -.
DR PATRIC; fig|511145.12.peg.1565; -.
DR EchoBASE; EB3557; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_10_2_6; -.
DR InParanoid; P77318; -.
DR OMA; PFTGLWQ; -.
DR PhylomeDB; P77318; -.
DR BioCyc; EcoCyc:G6788-MON; -.
DR PRO; PR:P77318; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..560
FT /note="Uncharacterized sulfatase YdeN"
FT /id="PRO_0000033449"
FT ACT_SITE 132
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 185
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
SQ SEQUENCE 560 AA; 62802 MW; 67ED7FF7696C7A9F CRC64;
MKSALKKSVV STSISLILAS GMAAFAAHAA DDVKLKATKT NVAFSDFTPT EYSTKGKPNI
IVLTMDDLGY GQLPFDKGSF DPKTMENREV VDTYKIGIDK AIEAAQKSTP TLLSLMDEGV
RFTNGYVAHG VSGPSRAAIM TGRAPARFGV YSNTDAQDGI PLTETFLPEL FQNHGYYTAA
VGKWHLSKIS NVPVPEDKQT RDYHDNFTTF SAEEWQPQNR GFDYFMGFHA AGTAYYNSPS
LFKNRERVPA KGYISDQLTD EAIGVVDRAK TLDQPFMLYL AYNAPHLPND NPAPDQYQKQ
FNTGSQTADN YYASVYSVDQ GVKRILEQLK KNGQYDNTII LFTSDNGAVI DGPLPLNGAQ
KGYKSQTYPG GTHTPMFMWW KGKLQPGNYD KLISAMDFYP TALDAADISI PKDLKLDGVS
LLPWLQDKKQ GEPHKNLTWI TSYSHWFDEE NIPFWDNYHK FVRHQSDDYP HNPNTEDLSQ
FSYTVRNNDY SLVYTVENNQ LGLYKLTDLQ QKDNLAAANP QVVKEMQGVV REFIDSSQPP
LSEVNQEKFN NIKKALSEAK
