ACYP_RHOPS
ID ACYP_RHOPS Reviewed; 99 AA.
AC Q135C2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=RPD_3091;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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 -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR EMBL; CP000283; ABE40317.1; -; Genomic_DNA.
DR AlphaFoldDB; Q135C2; -.
DR SMR; Q135C2; -.
DR STRING; 316057.RPD_3091; -.
DR EnsemblBacteria; ABE40317; ABE40317; RPD_3091.
DR KEGG; rpd:RPD_3091; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_3_2_5; -.
DR OMA; VGFRWSM; -.
DR OrthoDB; 2034659at2; -.
DR BioCyc; RPAL316057:RPD_RS15525-MON; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
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; PTHR47268; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..99
FT /note="Acylphosphatase"
FT /id="PRO_0000326788"
FT DOMAIN 5..97
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 99 AA; 10849 MW; 29480F561E2B9B06 CRC64;
MSTTIRQVMV RGRVQGVGYR AWLAMTAEAQ GLEGWVRNRR DGSVEALLAG RETVVAEMIS
RCRTGPSAAH VDEVIVEEAG QDALNLRYAG ERFSILSTL