ID ACYP_KLEP7 Reviewed; 95 AA.
AC A6T769;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=KPN78578_09790; ORFNames=KPN_01004;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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; CP000647; ABR76440.1; -; Genomic_DNA.
DR AlphaFoldDB; A6T769; -.
DR SMR; A6T769; -.
DR STRING; 272620.KPN_01004; -.
DR PaxDb; 272620-KPN_01004; -.
DR EnsemblBacteria; ABR76440; ABR76440; KPN_01004.
DR KEGG; kpn:KPN_01004; -.
DR HOGENOM; CLU_141932_1_2_6; -.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.100; -; 1.
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; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 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..95
FT /note="Acylphosphatase"
FT /id="PRO_0000326723"
FT DOMAIN 7..95
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 40
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
SQ SEQUENCE 95 AA; 10520 MW; A5653C88B52B2728 CRC64;
MIMASICTMA WVYGSVQGVG FRYSTQREAL QLGVTGYARN LDDGGVEVLV CGEAEQVEKL
IAWLKAGGPR SARVDRVLTE PHQPTRSWDK FAILY
//
