ACYP_COXBU
ID ACYP_COXBU Reviewed; 95 AA.
AC Q83AB0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=CBU_1995;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO91484.2; -; Genomic_DNA.
DR RefSeq; NP_820970.2; NC_002971.3.
DR RefSeq; WP_010958585.1; NC_002971.4.
DR PDB; 3TRG; X-ray; 1.60 A; A=1-95.
DR PDBsum; 3TRG; -.
DR AlphaFoldDB; Q83AB0; -.
DR SMR; Q83AB0; -.
DR STRING; 227377.CBU_1995; -.
DR DNASU; 1209908; -.
DR EnsemblBacteria; AAO91484; AAO91484; CBU_1995.
DR GeneID; 1209908; -.
DR KEGG; cbu:CBU_1995; -.
DR PATRIC; fig|227377.7.peg.1982; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_1_0_6; -.
DR OMA; VGFRWSM; -.
DR EvolutionaryTrace; Q83AB0; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR10029; PTHR10029; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..95
FT /note="Acylphosphatase"
FT /id="PRO_0000326693"
FT DOMAIN 10..95
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:3TRG"
FT STRAND 8..18
FT /evidence="ECO:0007829|PDB:3TRG"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3TRG"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3TRG"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3TRG"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:3TRG"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3TRG"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3TRG"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:3TRG"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3TRG"
SQ SEQUENCE 95 AA; 10908 MW; 8C719D0EB45DD768 CRC64;
MTQKEKNETC IHVTVSGKVQ GVFFRESVRK KAEELQLTGW VKNLSHGDVE LVACGERDSI
MILTEWLWEG PPQAAVSNVN WEEIVVEDYS DFRVR
