ACYP_DESVH
ID ACYP_DESVH Reviewed; 100 AA.
AC Q72CU1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=DVU_1192;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS95670.1; -; Genomic_DNA.
DR RefSeq; WP_010938488.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010411.1; NC_002937.3.
DR AlphaFoldDB; Q72CU1; -.
DR SMR; Q72CU1; -.
DR IntAct; Q72CU1; 1.
DR STRING; 882.DVU_1192; -.
DR PaxDb; Q72CU1; -.
DR EnsemblBacteria; AAS95670; AAS95670; DVU_1192.
DR KEGG; dvu:DVU_1192; -.
DR PATRIC; fig|882.5.peg.1116; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_3_2_7; -.
DR OMA; VGFRWSM; -.
DR PhylomeDB; Q72CU1; -.
DR Proteomes; UP000002194; 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..100
FT /note="Acylphosphatase"
FT /id="PRO_0000326702"
FT DOMAIN 3..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT REGION 76..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 100 AA; 11203 MW; 90B2FAE9F1F9C55D CRC64;
MPRRSYSVIG RVQGVGFRSW TRRTALRLDL RGWVRNEPDG TVRLCADGTD EALATLETAL
RKGPMFSRVD HVVKHDDPAH EGPLPDTFDI RFRAPGSASE
