ACYP_ENT38
ID ACYP_ENT38 Reviewed; 94 AA.
AC A4W8Y0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=acyP; OrderedLocusNames=Ent638_1480;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP60160.1; -; Genomic_DNA.
DR RefSeq; WP_012016877.1; NC_009436.1.
DR AlphaFoldDB; A4W8Y0; -.
DR SMR; A4W8Y0; -.
DR STRING; 399742.Ent638_1480; -.
DR EnsemblBacteria; ABP60160; ABP60160; Ent638_1480.
DR KEGG; ent:Ent638_1480; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_1_2_6; -.
DR OMA; VGFRWSM; -.
DR OrthoDB; 2034659at2; -.
DR Proteomes; UP000000230; 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 Hydrolase.
FT CHAIN 1..94
FT /note="Acylphosphatase"
FT /id="PRO_0000326705"
FT DOMAIN 6..94
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 39
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
SQ SEQUENCE 94 AA; 10520 MW; 8CDA795F1275E7F6 CRC64;
MMSKVCTIAW VHGTVQGVGF RYSTQREALQ LGLTGYARNL DDGSVEVVAC GEADNIEQLI
AWLKAGGPRS ARVEKVFTEP HQPDREYDKF SIRY
