ID A0A1Q7LM67_9CREN Unreviewed; 91 AA.
AC A0A1Q7LM67;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
GN ORFNames=AUJ07_11145 {ECO:0000313|EMBL:OLD01478.1};
OS Crenarchaeota archaeon 13_1_40CM_3_53_5.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805098 {ECO:0000313|EMBL:OLD01478.1, ECO:0000313|Proteomes:UP000186658};
RN [1] {ECO:0000313|EMBL:OLD01478.1, ECO:0000313|Proteomes:UP000186658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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|PROSITE-ProRule:PRU00520,
CC ECO:0000256|RuleBase:RU000553};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
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:OLD01478.1}.
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DR EMBL; MNGL01000077; OLD01478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7LM67; -.
DR STRING; 1805098.AUJ07_11145; -.
DR Proteomes; UP000186658; 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; 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}.
FT DOMAIN 4..91
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 19
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 91 AA; 10303 MW; 56E6605B051361B9 CRC64;
MEARAHLLIS GLVQGVLFRK RIMELARSKS INGWVRNLHD GRVEAVAEGE KDNIDALIQF
CKVGPPGAKV RSVDIEWSEF KSEFRGFKIL H
//
