ID G5QH09_SALRU Unreviewed; 93 AA.
AC G5QH09;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|HAMAP-Rule:MF_01450};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|HAMAP-Rule:MF_01450};
DE AltName: Full=Acylphosphate phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_01450};
GN Name=yccX {ECO:0000256|HAMAP-Rule:MF_01450};
GN ORFNames=LTSERUB_1736 {ECO:0000313|EMBL:EHC91447.1};
OS Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913081 {ECO:0000313|EMBL:EHC91447.1, ECO:0000313|Proteomes:UP000004903};
RN [1] {ECO:0000313|EMBL:EHC91447.1, ECO:0000313|Proteomes:UP000004903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-653 {ECO:0000313|EMBL:EHC91447.1,
RC ECO:0000313|Proteomes:UP000004903};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:0000256|ARBA:ARBA00000744, ECO:0000256|HAMAP-
CC Rule:MF_01450, ECO:0000256|PROSITE-ProRule:PRU00520,
CC ECO:0000256|RuleBase:RU000553};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|HAMAP-Rule:MF_01450,
CC ECO:0000256|RuleBase:RU004168}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC91447.1}.
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DR EMBL; AFCT01000663; EHC91447.1; -; Genomic_DNA.
DR AlphaFoldDB; G5QH09; -.
DR PATRIC; fig|913081.3.peg.1395; -.
DR Proteomes; UP000004903; Unassembled WGS sequence.
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 Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01450};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01450, ECO:0000256|PROSITE-
KW ProRule:PRU00520}.
FT DOMAIN 5..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01450,
FT ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01450,
FT ECO:0000256|PROSITE-ProRule:PRU00520"
FT DISULFID 5..49
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01450"
SQ SEQUENCE 93 AA; 10357 MW; 3DE3C26E4E15FFFD CRC64;
MSNVCIIAWV YGRVQGVGFR YTTQHEAQRL GLTGYAKNMD DGSVEVVVCG DAAQVEKLIK
WLKEGGPRSA RVDKILTEPH SPRETLTGFS IRY
//
