ACYP_SALAR
ID ACYP_SALAR Reviewed; 93 AA.
AC A9MHS1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=SARI_01929;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX21811.1; -; Genomic_DNA.
DR RefSeq; WP_000072888.1; NC_010067.1.
DR AlphaFoldDB; A9MHS1; -.
DR SMR; A9MHS1; -.
DR STRING; 41514.SARI_01929; -.
DR EnsemblBacteria; ABX21811; ABX21811; SARI_01929.
DR KEGG; ses:SARI_01929; -.
DR HOGENOM; CLU_141932_1_2_6; -.
DR OMA; VGFRWSM; -.
DR OrthoDB; 2034659at2; -.
DR Proteomes; UP000002084; 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..93
FT /note="Acylphosphatase"
FT /id="PRO_0000326795"
FT DOMAIN 5..93
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 93 AA; 10428 MW; 5C454A537C754B18 CRC64;
MSNVCTIAWI YGRVQGVGFR YTTQHEAQRL GLTGYAKNMD DGSVEVVACG DEAQVEKLIK
WLKEGGPRSA RVDKILTEPH SPHETLTDFS IRY
