ACYP2_DROME
ID ACYP2_DROME Reviewed; 102 AA.
AC Q9VF36; Q29QI6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Acylphosphatase-2;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase 2;
DE Short=AcPDro2;
GN Name=Acyp2 {ECO:0000312|EMBL:AAF55224.1}; ORFNames=CG18505;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF55224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF55224.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP CATALYTIC ACTIVITY, MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12560098; DOI=10.1016/s0014-5793(02)03901-7;
RA Degl'Innocenti D., Ramazzotti M., Marzocchini R., Chiti F., Raugei G.,
RA Ramponi G.;
RT "Characterization of a novel Drosophila melanogaster acylphosphatase.";
RL FEBS Lett. 535:171-174(2003).
RN [5] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=15159593; DOI=10.1107/s0907444904006808;
RA Zuccotti S., Rosano C., Ramazzotti M., Degl'Innocenti D., Stefani M.,
RA Manao G., Bolognesi M.;
RT "Three-dimensional structural characterization of a novel Drosophila
RT melanogaster acylphosphatase.";
RL Acta Crystallogr. D 60:1177-1179(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 Evidence={ECO:0000269|PubMed:12560098};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.80 mM for benzoylphosphate {ECO:0000269|PubMed:12560098};
CC pH dependence:
CC Optimum pH is 4.8-5.8. {ECO:0000269|PubMed:12560098};
CC -!- MASS SPECTROMETRY: Mass=11778; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12560098};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000269|PubMed:12560098, ECO:0000269|PubMed:15159593}.
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DR EMBL; AE014297; AAF55224.1; -; Genomic_DNA.
DR EMBL; BT024404; ABC86466.1; -; mRNA.
DR RefSeq; NP_001262612.1; NM_001275683.1.
DR RefSeq; NP_650491.1; NM_142234.2.
DR PDB; 1URR; X-ray; 1.50 A; A=1-102.
DR PDBsum; 1URR; -.
DR AlphaFoldDB; Q9VF36; -.
DR SMR; Q9VF36; -.
DR STRING; 7227.FBpp0082628; -.
DR PaxDb; Q9VF36; -.
DR PRIDE; Q9VF36; -.
DR DNASU; 41910; -.
DR EnsemblMetazoa; FBtr0083174; FBpp0082628; FBgn0038363.
DR EnsemblMetazoa; FBtr0334591; FBpp0306658; FBgn0038363.
DR GeneID; 41910; -.
DR KEGG; dme:Dmel_CG18505; -.
DR CTD; 98; -.
DR FlyBase; FBgn0038363; Acyp2.
DR VEuPathDB; VectorBase:FBgn0038363; -.
DR eggNOG; KOG3360; Eukaryota.
DR GeneTree; ENSGT00940000166472; -.
DR HOGENOM; CLU_141932_0_1_1; -.
DR InParanoid; Q9VF36; -.
DR OMA; TNGIMAG; -.
DR OrthoDB; 1502266at2759; -.
DR PhylomeDB; Q9VF36; -.
DR SABIO-RK; Q9VF36; -.
DR BioGRID-ORCS; 41910; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Acyp2; fly.
DR EvolutionaryTrace; Q9VF36; -.
DR GenomeRNAi; 41910; -.
DR PRO; PR:Q9VF36; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038363; Expressed in testis and 26 other tissues.
DR ExpressionAtlas; Q9VF36; baseline and differential.
DR Genevisible; Q9VF36; DM.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0003998; F:acylphosphatase activity; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
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; PS51160; ACYLPHOSPHATASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..102
FT /note="Acylphosphatase-2"
FT /id="PRO_0000158551"
FT DOMAIN 12..102
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 27
FT /evidence="ECO:0000303|PubMed:12560098"
FT ACT_SITE 45
FT /evidence="ECO:0000303|PubMed:12560098"
FT STRAND 10..20
FT /evidence="ECO:0007829|PDB:1URR"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1URR"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:1URR"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1URR"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1URR"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1URR"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1URR"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1URR"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1URR"
SQ SEQUENCE 102 AA; 11766 MW; 3CDC09E7FF96FBDE CRC64;
MAGSGVAKQI FALDFEIFGR VQGVFFRKHT SHEAKRLGVR GWCMNTRDGT VKGQLEAPMM
NLMEMKHWLE NNRIPNAKVS KAEFSQIQEI EDYTFTSFDI KH