ID A0A1C4GMG8_9ENTR Unreviewed; 93 AA.
AC A0A1C4GMG8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=GA0061070_10874 {ECO:0000313|EMBL:SCC69346.1};
OS Kosakonia oryziphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kosakonia.
OX NCBI_TaxID=1005667 {ECO:0000313|EMBL:SCC69346.1, ECO:0000313|Proteomes:UP000198515};
RN [1] {ECO:0000313|Proteomes:UP000198515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REICA_142 {ECO:0000313|Proteomes:UP000198515};
RA Varghese N., Submissions Spin;
RL Submitted (AUG-2016) 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: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}.
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DR EMBL; FMBC01000087; SCC69346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4GMG8; -.
DR OrthoDB; 5295388at2; -.
DR Proteomes; UP000198515; 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 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"
SQ SEQUENCE 93 AA; 10383 MW; 5428AC06BF6A6A06 CRC64;
MTQVCTIAWV HGMVQGVGFR YSTQYEAQRL GLTGYARNLD DGSVEVVACG EAENVDKLVA
WLKAGGPRSA RVERVLTEPH QPGREWKNFG IRY
//
