ACYP_SHIFL
ID ACYP_SHIFL Reviewed; 92 AA.
AC Q83LL9; Q7UD11;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 4.
DT 25-MAY-2022, entry version 115.
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};
GN OrderedLocusNames=SF0969, S1036;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42598.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16484.1; -; Genomic_DNA.
DR RefSeq; NP_706891.2; NC_004337.2.
DR RefSeq; WP_000034173.1; NZ_WPGW01000043.1.
DR AlphaFoldDB; Q83LL9; -.
DR BMRB; Q83LL9; -.
DR SMR; Q83LL9; -.
DR STRING; 198214.SF0969; -.
DR EnsemblBacteria; AAN42598; AAN42598; SF0969.
DR EnsemblBacteria; AAP16484; AAP16484; S1036.
DR GeneID; 1023958; -.
DR KEGG; sfl:SF0969; -.
DR KEGG; sfx:S1036; -.
DR PATRIC; fig|198214.7.peg.1129; -.
DR HOGENOM; CLU_141932_1_2_6; -.
DR OMA; VGFRWSM; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
FT CHAIN 1..92
FT /note="Acylphosphatase"
FT /id="PRO_0000326802"
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
