ID A0A1Y6CR84_9PROT Unreviewed; 91 AA.
AC A0A1Y6CR84;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Acylphosphatase {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=SAMN05428998_1494 {ECO:0000313|EMBL:SMF83245.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF83245.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SMF83245.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SMF83245.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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|PROSITE-
CC ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
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DR EMBL; FWZX01000049; SMF83245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6CR84; -.
DR STRING; 560819.SAMN05428998_1494; -.
DR Proteomes; UP000192917; Unassembled WGS sequence.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
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|PROSITE-ProRule:PRU00520,
KW ECO:0000256|RuleBase:RU000553};
KW Reference proteome {ECO:0000313|Proteomes:UP000192917}.
FT DOMAIN 3..89
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 91 AA; 10034 MW; 3B2E79468899287F CRC64;
MRQVLARVHG RVQGVWFRAW TVQEAQRLGL DGWVRNRRDG TVEALFAGAA AAVEEMLRLC
HDGPLHARVV AVETAETDEA APAGFEQRPT A
//
