ID A0A0S8CGC8_9BACT Unreviewed; 93 AA.
AC A0A0S8CGC8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 24.
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=AMK69_19355 {ECO:0000313|EMBL:KPK22658.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK22658.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK22658.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK22658.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPK22658.1}.
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DR EMBL; LJNR01000407; KPK22658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CGC8; -.
DR PATRIC; fig|1704023.3.peg.2720; -.
DR Proteomes; UP000051394; 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}.
FT DOMAIN 5..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 93 AA; 10612 MW; 9FF955256446E5C0 CRC64;
MKNVRCHVRI DGRVQGVCFR MDTRRAALER NLTGWVRNLP DGGVEAVFEG TQVDVKSMLK
WCEIGPPLAH VRKTTVAWEP YTGEFDTFEI TFA
//
