ID A0A0F2LA78_9CREN Unreviewed; 566 AA.
AC A0A0F2LA78;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=TU35_00165 {ECO:0000313|EMBL:KJR74452.1};
OS Thermoproteus sp. AZ2.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=1609232 {ECO:0000313|EMBL:KJR74452.1, ECO:0000313|Proteomes:UP000033636};
RN [1] {ECO:0000313|EMBL:KJR74452.1, ECO:0000313|Proteomes:UP000033636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-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|PROSITE-ProRule:PRU00520};
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:KJR74452.1}.
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DR EMBL; JZWT01000001; KJR74452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2LA78; -.
DR PATRIC; fig|1609232.3.peg.34; -.
DR Proteomes; UP000033636; Unassembled WGS sequence.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR036676; PurM-like_C_sf.
DR NCBIfam; NF038049; SelD_rel_HyperS; 1.
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 SUPFAM; SSF56042; PurM C-terminal 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}.
FT DOMAIN 482..566
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 515
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 566 AA; 62658 MW; 28B5963DDF3FCF0E CRC64;
MRAEFKERVK LYREAGIAIE SLSLGCSVKV DLYDVLYPAI QLLSGELSRL NLVIAPREDA
AIMRGESAEL TRLYLDVEEP KIDPALIESL APDLAIVLVQ LYMAKASSPD KFAEYAARLY
RALGSSRHRV WLGKGHSIVS TKRGSEFFMV DFLKTRGTGY ILANNDTIQV IDPSEDLDSP
LQAAVAVNNA LNDLYIKGVY KDVHIAPVYD APQQYLDGVR KAVLSHAAGL GKVVDAPQPN
KGYLLLGATA WGYLDREPPT FYKHIDKGFV VLVTRPFGEL AYFTTYVAIN TDDELLKAFE
REVMTLDELE REKKRVLELM ATPNVEIAKV IYKYLPELGD RFRPEEHIAA TIDVSGPGIF
VFKEVGERAE ADVELFDVPL LGPKISRFAA QNYIMPDATA GTNGAVAIFV HEALADELLK
ELRKIPGLSP RVIGRVVGRG EGKLIVPRDA LDYISSAKLR GKLEAQAEVL SGLSTRAKRP
GRAKIVFEGE VQGVGFRPLA RAKAKALGLY GYAKNLPDGR VEVVVEGDVE RIKRLAEVLC
PEGANCRVSE MTWEEYRGEF KDFDIL
//
