ACYP_SHIBS
ID ACYP_SHIBS Reviewed; 92 AA.
AC Q31YN1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Acylphosphatase {ECO:0000255|HAMAP-Rule:MF_01450};
DE EC=3.6.1.7 {ECO:0000255|HAMAP-Rule:MF_01450};
DE AltName: Full=Acylphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01450};
GN Name=yccX {ECO:0000255|HAMAP-Rule:MF_01450}; OrderedLocusNames=SBO_2263;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01450};
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000255|HAMAP-
CC Rule:MF_01450}.
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DR EMBL; CP000036; ABB66827.1; -; Genomic_DNA.
DR RefSeq; WP_000034173.1; NC_007613.1.
DR AlphaFoldDB; Q31YN1; -.
DR BMRB; Q31YN1; -.
DR SMR; Q31YN1; -.
DR EnsemblBacteria; ABB66827; ABB66827; SBO_2263.
DR KEGG; sbo:SBO_2263; -.
DR HOGENOM; CLU_141932_1_2_6; -.
DR OMA; VGFRWSM; -.
DR Proteomes; UP000007067; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01450; Acylphosphatase_entero; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR028627; Acylphosphatase_bac.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR47268; PTHR47268; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase.
FT CHAIN 1..92
FT /note="Acylphosphatase"
FT /id="PRO_0000326801"
FT DOMAIN 5..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 38
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT DISULFID 5..49
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
SQ SEQUENCE 92 AA; 10328 MW; 7272359F06404DCF CRC64;
MSKICIIAWI YGRVQGVGFR YTTQYEAKRL GLTGYAKNLD DGSVEVVACG EEGQVEKLMQ
WLKSGGPRSA RVERVLSEPH HPSGELTDFR IR
