ACYP_GEOMG
ID ACYP_GEOMG Reviewed; 93 AA.
AC Q39S27;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=Gmet_2729;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) 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; CP000148; ABB32947.1; -; Genomic_DNA.
DR RefSeq; WP_004511731.1; NC_007517.1.
DR AlphaFoldDB; Q39S27; -.
DR SMR; Q39S27; -.
DR STRING; 269799.Gmet_2729; -.
DR EnsemblBacteria; ABB32947; ABB32947; Gmet_2729.
DR KEGG; gme:Gmet_2729; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_1_0_7; -.
DR OMA; GTVEAMF; -.
DR OrthoDB; 2034659at2; -.
DR Proteomes; UP000007073; 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 PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; SSF54975; 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; Reference proteome.
FT CHAIN 1..93
FT /note="Acylphosphatase"
FT /id="PRO_0000326715"
FT DOMAIN 6..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 93 AA; 10610 MW; C7059FEAE90525D8 CRC64;
MTMKIRAIVT VKGLVQGVAF RHHTVLQGNQ LRVTGWVKNL PNGDVQGCFE GDETDVQALV
EWCHHGPSRA RVDRVIVERK SFRGEFDTFD VRY
