ID A0A0J6BD86_9SYNE Unreviewed; 82 AA.
AC A0A0J6BD86;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 28-JUN-2023, entry version 28.
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=SYNGFB01_10155 {ECO:0000313|EMBL:KMM16523.1};
OS Synechococcus sp. GFB01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1662190 {ECO:0000313|EMBL:KMM16523.1, ECO:0000313|Proteomes:UP000035901};
RN [1] {ECO:0000313|EMBL:KMM16523.1, ECO:0000313|Proteomes:UP000035901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFB01 {ECO:0000313|EMBL:KMM16523.1,
RC ECO:0000313|Proteomes:UP000035901};
RA Guimaraes P.I., Leao T.F., de Melo A.G., Ramos R.T., Silva A., Fiore M.F.,
RA Schneider M.P.;
RT "Draft genome of the picocyanobacterium Synechococcus sp. strain GFB01
RT isolated from a freshwater lagoon of the Brazilian Amazon.";
RL Submitted (JUN-2015) 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};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, 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:KMM16523.1}.
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DR EMBL; LFEK01000110; KMM16523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6BD86; -.
DR STRING; 1662190.SYNGFB01_10155; -.
DR PATRIC; fig|1662190.3.peg.228; -.
DR Proteomes; UP000035901; 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 SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000035901}.
FT DOMAIN 1..82
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 11
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 82 AA; 8852 MW; 46EC7F7A772FF920 CRC64;
MRGRVQGVGY RAGCRDRARD LGLGGWVRNL PDGSVEVEAE GTAEQLAELR LWCEHGPEGA
GVSGVGISQI GLTGQDWFEV RR
//
