ID D3PBZ5_DEFDS Unreviewed; 90 AA.
AC D3PBZ5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=DEFDS_0637 {ECO:0000313|EMBL:BAI80118.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI80118.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI80118.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
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; AP011529; BAI80118.1; -; Genomic_DNA.
DR RefSeq; WP_013007366.1; NC_013939.1.
DR AlphaFoldDB; D3PBZ5; -.
DR STRING; 639282.DEFDS_0637; -.
DR KEGG; ddf:DEFDS_0637; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_2_1_0; -.
DR OrthoDB; 9808093at2; -.
DR Proteomes; UP000001520; 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 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:UP000001520}.
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; 10141 MW; 186EF18262E86D00 CRC64;
MKRLHAIVSG RVQGVGFRAF VYDKALNLNL KGYVKNLPDG TVEVDAEGDE KSLIELLSHL
RVGPSLSNVT NIDFEITDKL VNYSDFRIRY
//
