ID A0A0U5APB3_9BACT Unreviewed; 90 AA.
AC A0A0U5APB3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=THC_1576 {ECO:0000313|EMBL:BAU23940.1};
OS Caldimicrobium thiodismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23940.1, ECO:0000313|Proteomes:UP000068196};
RN [1] {ECO:0000313|EMBL:BAU23940.1, ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|EMBL:BAU23940.1,
RC ECO:0000313|Proteomes:UP000068196};
RX PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring, and emended description of the genus
RT Caldimicrobium.";
RL Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN [2] {ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(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|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}.
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DR EMBL; AP014945; BAU23940.1; -; Genomic_DNA.
DR RefSeq; WP_068515778.1; NZ_AP014945.1.
DR AlphaFoldDB; A0A0U5APB3; -.
DR STRING; 1653476.THC_1576; -.
DR KEGG; cthi:THC_1576; -.
DR PATRIC; fig|1653476.3.peg.1638; -.
DR OrthoDB; 9808093at2; -.
DR Proteomes; UP000068196; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000068196}.
FT DOMAIN 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 90 AA; 10509 MW; 6F0D411F44C03B37 CRC64;
MKRIRVLISG RVQGVFFRAY TKEEAERLGL KGWVRNLPDG RVEALFEGEE KAVAEMLKWC
HRGSPASVVT KVETFEEHYT GEFKDFKIRY
//
