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Database: UniProt
Entry: A0A0U4BBN6_9ACTN
LinkDB: A0A0U4BBN6_9ACTN
Original site: A0A0U4BBN6_9ACTN 
ID   A0A0U4BBN6_9ACTN        Unreviewed;        89 AA.
AC   A0A0U4BBN6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=AERYTH_11555 {ECO:0000313|EMBL:ALX05289.1};
OS   Aeromicrobium erythreum.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX05289.1, ECO:0000313|Proteomes:UP000067689};
RN   [1] {ECO:0000313|EMBL:ALX05289.1, ECO:0000313|Proteomes:UP000067689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR18 {ECO:0000313|EMBL:ALX05289.1,
RC   ECO:0000313|Proteomes:UP000067689};
RX   PubMed=1883712;
RA   Miller E.S., Woese C.R., Brenner S.;
RT   "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT   strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL   Int. J. Syst. Bacteriol. 41:363-368(1991).
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; CP011502; ALX05289.1; -; Genomic_DNA.
DR   RefSeq; WP_067858746.1; NZ_CP011502.1.
DR   AlphaFoldDB; A0A0U4BBN6; -.
DR   STRING; 2041.AERYTH_11555; -.
DR   KEGG; aer:AERYTH_11555; -.
DR   PATRIC; fig|2041.4.peg.2414; -.
DR   OrthoDB; 3182027at2; -.
DR   Proteomes; UP000067689; 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; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067689}.
FT   DOMAIN          3..89
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   89 AA;  9706 MW;  9CC500F7966FCAD2 CRC64;
     MIRRHVVVSG HVQGVFYRAS LEREAHAAGV AGWVRNRDDG TVEAVLEGEP AAVERVLAWC
     RQGPPRAEVA DVAVEEEEPV GETGFRTRG
//
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