ID Q32DN9_SHIDS Unreviewed; 184 AA.
AC Q32DN9;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN Name=yfcE {ECO:0000313|EMBL:ABB62566.1};
GN OrderedLocusNames=SDY_2496 {ECO:0000313|EMBL:ABB62566.1};
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB62566.1, ECO:0000313|Proteomes:UP000002716};
RN [1] {ECO:0000313|EMBL:ABB62566.1, ECO:0000313|Proteomes:UP000002716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB62566.1,
RC ECO:0000313|Proteomes:UP000002716};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU362039};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE
CC family. {ECO:0000256|ARBA:ARBA00008950, ECO:0000256|RuleBase:RU362039}.
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DR EMBL; CP000034; ABB62566.1; -; Genomic_DNA.
DR RefSeq; YP_404057.1; NC_007606.1.
DR AlphaFoldDB; Q32DN9; -.
DR STRING; 300267.SDY_2496; -.
DR EnsemblBacteria; ABB62566; ABB62566; SDY_2496.
DR KEGG; sdy:SDY_2496; -.
DR PATRIC; fig|300267.13.peg.3008; -.
DR HOGENOM; CLU_063749_1_1_6; -.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00841; MPP_YfcE; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041802; MPP_YfcE.
DR InterPro; IPR020935; PdiEstase_YfcE_CS.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR NCBIfam; TIGR00040; yfcE; 1.
DR PANTHER; PTHR11124:SF26; PHOSPHODIESTERASE YFCE; 1.
DR PANTHER; PTHR11124; VACUOLAR SORTING PROTEIN VPS29; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS01269; UPF0025; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|RuleBase:RU362039};
KW Reference proteome {ECO:0000313|Proteomes:UP000002716}.
FT DOMAIN 2..162
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF12850"
SQ SEQUENCE 184 AA; 20106 MW; 15C5AA14F95405A9 CRC64;
MMKLMFASDI HGSLPATERV LELFAQSGAQ WLVILGDVLN HGPRNALPEG YAPAKVAERL
NEVAHKVIAV RGNCDSEVDQ MLLHFPITAP WQQVLLEKQR LFLTHGHLFG PENLPALNQN
DVLVFGHTHL PVAEQRGEIF HFNPGSVSIP KGGNPASYGM LDNDVLSVIA LNDQSIIAQV
AINP
//
