ID D7AQ33_THEM3 Unreviewed; 90 AA.
AC D7AQ33;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 OrderedLocusNames=Tmath_1565 {ECO:0000313|EMBL:ADH61274.1};
OS Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS 53645 / CIP 108742 / A3).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH61274.1, ECO:0000313|Proteomes:UP000002064};
RN [1] {ECO:0000313|EMBL:ADH61274.1, ECO:0000313|Proteomes:UP000002064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11426 / CIP 108742 / A3
RC {ECO:0000313|Proteomes:UP000002064};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT mathranii str. A3.";
RL Submitted (MAY-2010) 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}.
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DR EMBL; CP002032; ADH61274.1; -; Genomic_DNA.
DR RefSeq; WP_012995540.1; NC_014209.1.
DR AlphaFoldDB; D7AQ33; -.
DR STRING; 583358.Tmath_1565; -.
DR KEGG; tmt:Tmath_1565; -.
DR HOGENOM; CLU_141932_3_2_9; -.
DR Proteomes; UP000002064; Chromosome.
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}.
FT DOMAIN 4..90
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 90 AA; 10386 MW; E3966F1010C48299 CRC64;
MKKTVHLRIT GHVQGVGLRY SVYQKAVSLG IAGYAENLYD GSVEVVAEGE EENIKELINF
IKTGLRWARV DNVEENWSNY KGEYRDFRIY
//
