ID R0P792_STRMT Unreviewed; 92 AA.
AC R0P792;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=D065_02291 {ECO:0000313|EMBL:EOB33283.1};
OS Streptococcus mitis 13/39.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1239793 {ECO:0000313|EMBL:EOB33283.1, ECO:0000313|Proteomes:UP000013315};
RN [1] {ECO:0000313|EMBL:EOB33283.1, ECO:0000313|Proteomes:UP000013315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13/39 {ECO:0000313|EMBL:EOB33283.1,
RC ECO:0000313|Proteomes:UP000013315};
RA Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Semashko T.A.,
RA Karpova I.Y.U., Larin A.K., Ischenko D.S., Alekseev D.G., Klimova E.A.,
RA Filimonova A.V., Savinova T.A., Filimonova O.Y.U., Dubovickaya V.A.,
RA Sidorenko S.V., Govorun V.M.;
RL Submitted (APR-2013) 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:EOB33283.1}.
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DR EMBL; AQTU01000005; EOB33283.1; -; Genomic_DNA.
DR AlphaFoldDB; R0P792; -.
DR PATRIC; fig|1239793.3.peg.444; -.
DR Proteomes; UP000013315; 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 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; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520,
KW ECO:0000313|EMBL:EOB33283.1}.
FT DOMAIN 3..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 92 AA; 10166 MW; C12CE3131E0E9C0D CRC64;
MQKVRMIAQG KVQGVGFRWG VYSLALEIGG ITGRVWNNDD GTVEILAQAD SSATMAKFIQ
EIRKGPTPFS KVSYLDVKLS NFPPYPDFKI AN
//
