DNAT2_DROME
ID DNAT2_DROME Reviewed; 216 AA.
AC Q9VMG0; Q4V4G0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Arylalkylamine N-acetyltransferase-like 2 {ECO:0000312|FlyBase:FBgn0031791};
DE Short=AANAT2 {ECO:0000303|PubMed:11098219};
DE EC=2.3.1.87 {ECO:0000255|PROSITE-ProRule:PRU00532, ECO:0000269|PubMed:11098219, ECO:0000269|PubMed:24444601, ECO:0000269|PubMed:31385627};
DE AltName: Full=Arylalkylamine N-acyltransferase-like 2 {ECO:0000303|PubMed:24444601};
DE EC=2.3.2.- {ECO:0000269|PubMed:24444601, ECO:0000269|PubMed:31385627};
GN Name=AANATL2 {ECO:0000303|PubMed:31385627,
GN ECO:0000312|FlyBase:FBgn0031791};
GN Synonyms=aaNAT2 {ECO:0000312|FlyBase:FBgn0031791};
GN ORFNames=CG9486 {ECO:0000312|FlyBase:FBgn0031791};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAY55462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 174-184 AND 189-192, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=11098219; DOI=10.1089/10445490050199081;
RA Amherd R., Hintermann E., Walz D., Affolter M., Meyer U.A.;
RT "Purification, cloning, and characterization of a second arylalkylamine N-
RT acetyltransferase from Drosophila melanogaster.";
RL DNA Cell Biol. 19:697-705(2000).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=24444601; DOI=10.1016/j.febslet.2013.12.027;
RA Dempsey D.R., Jeffries K.A., Anderson R.L., Carpenter A.M.,
RA Rodriquez Opsina S., Merkler D.J.;
RT "Identification of an arylalkylamine N-acyltransferase from Drosophila
RT melanogaster that catalyzes the formation of long-chain N-acylserotonins.";
RL FEBS Lett. 588:594-599(2014).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLU-29; PRO-30; ARG-138; SER-167; SER-171
RP AND HIS-206.
RX PubMed=26476413; DOI=10.1016/j.ibmb.2015.10.003;
RA Dempsey D.R., Carpenter A.M., Ospina S.R., Merkler D.J.;
RT "Probing the chemical mechanism and critical regulatory amino acid residues
RT of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.";
RL Insect Biochem. Mol. Biol. 66:1-12(2015).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31385627; DOI=10.1002/arch.21608;
RA Anderson R.L., Wallis D.J., Aguirre A., Holliday D., Merkler D.J.;
RT "Knockdown of arylalkylamine N-acetyltransferase-like 2 in Drosophila
RT melanogaster.";
RL Arch. Insect Biochem. Physiol. 102:e21608-e21608(2019).
CC -!- FUNCTION: Catalyzes the formation of long-chain N-acylserotonins and N-
CC acyldopamines, which are important cellular signaling lipids
CC (PubMed:24444601, PubMed:31385627). Catalyzes in vitro the formation of
CC various N-acetyl-2-arylethylamines such as N-acetyltryptamine and
CC melatonin (PubMed:11098219, PubMed:26476413).
CC {ECO:0000269|PubMed:11098219, ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413, ECO:0000269|PubMed:31385627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-arylethylamine + acetyl-CoA = CoA + H(+) + N-acetyl-2-
CC arylethylamine; Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:77827; EC=2.3.1.87;
CC Evidence={ECO:0000269|PubMed:11098219, ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413, ECO:0000269|PubMed:31385627};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20498;
CC Evidence={ECO:0000305|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + serotonin = CoA + H(+) + N-acetylserotonin;
CC Xref=Rhea:RHEA:25217, ChEBI:CHEBI:15378, ChEBI:CHEBI:17697,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:350546;
CC EC=2.3.1.87; Evidence={ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25218;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + serotonin = CoA + H(+) + N-butanoylserotonin;
CC Xref=Rhea:RHEA:66164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:134070, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66165;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + serotonin = CoA + H(+) + N-hexadecanoyl-
CC serotonin; Xref=Rhea:RHEA:51384, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:134059,
CC ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:24444601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51385;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + serotonin = CoA + H(+) + N-octadecanoyl-
CC serotonin; Xref=Rhea:RHEA:51400, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:134065,
CC ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51401;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + serotonin = CoA + H(+) + N-(9Z-
CC octadecenoyl)-serotonin; Xref=Rhea:RHEA:51392, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:134064,
CC ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51393;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + serotonin = CoA + H(+)
CC + N-[(5Z,8Z,11Z,14Z)-eicosatetraenoyl]-serotonin;
CC Xref=Rhea:RHEA:51396, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:132255, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000269|PubMed:24444601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51397;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + dopamine = CoA + H(+) + N-acetyl-dopamine;
CC Xref=Rhea:RHEA:51388, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:59905, ChEBI:CHEBI:125678;
CC Evidence={ECO:0000269|PubMed:24444601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51389;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + hexadecanoyl-CoA = CoA + H(+) + N-hexadecanoyl-
CC dopamine; Xref=Rhea:RHEA:51376, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:59905, ChEBI:CHEBI:134058;
CC Evidence={ECO:0000269|PubMed:24444601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51377;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + dopamine = CoA + H(+) + N-(9Z-
CC octadecanoyl)-dopamine; Xref=Rhea:RHEA:51380, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31883, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:24444601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51381;
CC Evidence={ECO:0000269|PubMed:24444601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + tyramine = CoA + H(+) + N-acetyltyramine;
CC Xref=Rhea:RHEA:66136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:125610, ChEBI:CHEBI:327995;
CC Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66137;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + tyramine = CoA + H(+) + N-butanoyltyramine;
CC Xref=Rhea:RHEA:66156, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:166900, ChEBI:CHEBI:327995;
CC Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66157;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + octopamine = CoA + H(+) + N-acetyloctopamine;
CC Xref=Rhea:RHEA:66140, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58025, ChEBI:CHEBI:125358;
CC Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66141;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methoxytryptamine + acetyl-CoA = CoA + H(+) + melatonin;
CC Xref=Rhea:RHEA:66144, ChEBI:CHEBI:15378, ChEBI:CHEBI:16796,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:166874;
CC Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66145;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + acetyl-CoA = CoA + H(+) + N-(2-
CC phenylethyl)acetamide; Xref=Rhea:RHEA:66148, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18177, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:225237; Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66149;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + noradrenaline = CoA + H(+) + N-
CC acetylnoradrenaline; Xref=Rhea:RHEA:66152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:166875,
CC ChEBI:CHEBI:166902; Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66153;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + tryptamine = CoA + H(+) + N-acetyltryptamine;
CC Xref=Rhea:RHEA:66196, ChEBI:CHEBI:15378, ChEBI:CHEBI:55515,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57887;
CC Evidence={ECO:0000269|PubMed:26476413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66197;
CC Evidence={ECO:0000305|PubMed:26476413};
CC -!- ACTIVITY REGULATION: When length of the acyl-CoA aliphatic chain is
CC increased, it begins to occupy the binding site for the amine
CC substrate, leading to non-productive amine binding which results in a
CC decrease in the rate of catalysis (PubMed:26476413). Inhibited by
CC tyrosol (an analog of tyramine) (PubMed:26476413). Tyramine or
CC octopamine are not substrates when the acyl acceptor is oleoyl-CoA
CC (PubMed:24444601). {ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.2 uM for tryptamine (for the enzyme without substrate bound to
CC the regulatory site and with acetyl CoA as cosubstrate)
CC {ECO:0000269|PubMed:11098219};
CC KM=0.6 mM for tryptamine (for the enzyme with substrate bound to the
CC regulatory site and with acetyl CoA as cosubstrate)
CC {ECO:0000269|PubMed:11098219};
CC KM=6.1 uM for acetyl-CoA (at pH 8 and with serotonin as cosubstrate)
CC {ECO:0000269|PubMed:24444601};
CC KM=1.8 uM for butanoyl-CoA (butyryl-CoA) (at pH 8 and with serotonin
CC as cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=9.9 uM for hexadecanoyl-CoA (palmitoyl-CoA) (at pH 8 and with
CC serotonin as cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=6.0 uM for octadecanoyl-CoA (stearoyl-CoA) (at pH 8 and with
CC serotonin as cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=3.6 uM for (9Z)-octadecenoyl-CoA (oleoyl-CoA) (at pH 8 and with
CC serotonin as cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=1.9 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA (arachidonoyl-CoA)
CC (at pH 8 and with serotonin as cosubstrate)
CC {ECO:0000269|PubMed:24444601};
CC KM=7.2 uM for serotonin (at pH 8 and with acetyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:24444601};
CC KM=2.9 uM for serotonin (at pH 8 and with butanoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=870 uM for serotonin (at pH 8 and with palmitoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=350 uM for serotonin (at pH 8 and with stearoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=490 uM for serotonin (at pH 8 and with oleoyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:24444601};
CC KM=460 uM for serotonin (at pH 8 and with arachidonoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=42 uM for dopamine (at pH 8 and with acetyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:24444601};
CC KM=1.1 uM for dopamine (at pH 8 and with palmitoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:24444601};
CC KM=7 uM for serotonin (at pH 8 and with acetyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:26476413};
CC KM=14 uM for tryptamine (at pH 8 and with acetyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:26476413};
CC KM=5 uM for tyramine (at pH 8 and with acetyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:26476413};
CC KM=35 uM for 2-phenylethylamine (at pH 8 and with acetyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:26476413};
CC KM=27 uM for noradrenaline (at pH 8 and with acetyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:26476413};
CC KM=25 uM for 5-methoxytryptamine (at pH 8 and with acetyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:26476413};
CC KM=78 uM for octapamine (at pH 8 and with acetyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:26476413};
CC KM=1.5 uM for acetyl-CoA (at pH 8 and with tyramine as cosubstrate)
CC {ECO:0000269|PubMed:26476413};
CC Note=kcat is 1.3 sec(-1) for acetyl-CoA (at pH 8 and with serotonine
CC as cosubstrate) (PubMed:24444601). kcat is 0.33 sec(-1) for butanoyl-
CC CoA (at pH 8 and with serotonine as cosubstrate) (PubMed:24444601).
CC kcat is 0.16 sec(-1) for palmitoyl-CoA (at pH 8 and with serotonine
CC as cosubstrate) (PubMed:24444601). kcat is 0.059 sec(-1) for steroyl-
CC CoA (at pH 8 and with serotonine as cosubstrate) (PubMed:24444601).
CC kcat is 0.075 sec(-1) for oleoyl-CoA (at pH 8 and with serotonine as
CC cosubstrate) (PubMed:24444601). kcat is 0.043 sec(-1) for
CC arachidonoyl-CoA (at pH 8 and with serotonine as cosubstrate)
CC (PubMed:24444601). kcat is 2.4 sec(-1) for serotonine (at pH 8 and
CC with acetyl-CoA as cosubstrate) (PubMed:24444601). kcat is 0.52 sec(-
CC 1) for serotonine (at pH 8 and with butanoyl-CoA as cosubstrate)
CC (PubMed:24444601). kcat is 0.15 sec(-1) for serotonine (at pH 8 and
CC with palmitoyl-CoA as cosubstrate) (PubMed:24444601). kcat is 0.057
CC sec(-1) for serotonine (at pH 8 and with steroyl-CoA as cosubstrate)
CC (PubMed:24444601). kcat is 0.030 sec(-1) for serotonine (at pH 8 and
CC with arachidonoyl-CoA as cosubstrate) (PubMed:24444601). kcat is 7
CC sec(-1) for dopamine (at pH 8 and with acetyl-CoA as cosubstrate)
CC (PubMed:24444601). kcat is 0.14 sec(-1) for dopamine (at pH 8 and
CC with palmitoyl-CoA as cosubstrate) (PubMed:24444601). kcat is 0.058
CC sec(-1) for dopamine (at pH 8 and with oleoyl-CoA as cosubstrate)
CC (PubMed:24444601). kcat is 2.4 sec(-1) for serotonin (at pH 8 and
CC with acetyl-CoA as cosubstrate) (PubMed:26476413). kcat is 4.3 sec(-
CC 1) for tryptamine (at pH 8 and with acetyl-CoA as cosubstrate)
CC (PubMed:26476413). kcat is 1.5 sec(-1) for tyramine (at pH 8 and with
CC acetyl-CoA as cosubstrate) (PubMed:26476413). kcat is 7.3 sec(-1) for
CC 2-phenylethylamine (at pH 8 and with acetyl-CoA as cosubstrate)
CC (PubMed:26476413). kcat is 5.6 sec(-1) for noradrenaline (at pH 8 and
CC with acetyl-CoA as cosubstrate) (PubMed:26476413). kcat is 2.6 sec(-
CC 1) for 5-methoxytryptamine (at pH 8 and with acetyl-CoA as
CC cosubstrate) (PubMed:26476413). kcat is 2.3 sec(-1) for octapamine
CC (at pH 8 and with acetyl-CoA as cosubstrate) (PubMed:26476413). kcat
CC is 1.6 sec(-1) for acetyl-CoA (at pH 8 and with tyramine as
CC cosubstrate) (PubMed:26476413). {ECO:0000269|PubMed:24444601,
CC ECO:0000269|PubMed:26476413};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:26476413};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000269|PubMed:24444601}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:31385627}.
CC -!- TISSUE SPECIFICITY: Expressed in all stages except early embryos
CC (PubMed:11098219). Expressed in thorax-abdomen (PubMed:24444601).
CC {ECO:0000269|PubMed:11098219, ECO:0000269|PubMed:24444601}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in decreased
CC levels of N-palmitoyldopamine (PALDA) and N-oleoylethanolamine and
CC higher levels of N-palmitoyl-derived fatty acid amides (FAAs), N-
CC palmitoylglycine, palmitamide and palmitoleamide.
CC {ECO:0000269|PubMed:31385627}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY55462.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF52358.1; -; Genomic_DNA.
DR EMBL; AE014134; AHN54182.1; -; Genomic_DNA.
DR EMBL; BT023046; AAY55462.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285667.1; NM_001298738.1.
DR RefSeq; NP_609005.1; NM_135161.3.
DR AlphaFoldDB; Q9VMG0; -.
DR SMR; Q9VMG0; -.
DR STRING; 7227.FBpp0078873; -.
DR SwissLipids; SLP:000001662; -.
DR PaxDb; Q9VMG0; -.
DR EnsemblMetazoa; FBtr0079243; FBpp0078873; FBgn0031791.
DR EnsemblMetazoa; FBtr0340167; FBpp0309152; FBgn0031791.
DR GeneID; 33874; -.
DR KEGG; dme:Dmel_CG9486; -.
DR UCSC; CG9486-RA; d. melanogaster.
DR CTD; 33874; -.
DR FlyBase; FBgn0031791; AANATL2.
DR VEuPathDB; VectorBase:FBgn0031791; -.
DR eggNOG; ENOG502SFIM; Eukaryota.
DR GeneTree; ENSGT00940000164149; -.
DR HOGENOM; CLU_085834_2_0_1; -.
DR InParanoid; Q9VMG0; -.
DR OMA; LYLYMLG; -.
DR OrthoDB; 1185856at2759; -.
DR PhylomeDB; Q9VMG0; -.
DR BRENDA; 2.3.1.87; 1994.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA00837; UER00815.
DR BioGRID-ORCS; 33874; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33874; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031791; Expressed in oviduct (Drosophila) and 19 other tissues.
DR ExpressionAtlas; Q9VMG0; baseline and differential.
DR GO; GO:0019186; F:acyl-CoA N-acyltransferase activity; IDA:FlyBase.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030187; P:melatonin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Reference proteome;
KW Transferase.
FT CHAIN 1..216
FT /note="Arylalkylamine N-acetyltransferase-like 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452802"
FT DOMAIN 4..216
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT SITE 29
FT /note="Regulates amine substrate binding"
FT /evidence="ECO:0000269|PubMed:26476413"
FT SITE 30
FT /note="Regulates catalysis and binding of the amine
FT substrate"
FT /evidence="ECO:0000269|PubMed:26476413"
FT MUTAGEN 29
FT /note="E->A: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:26476413"
FT MUTAGEN 30
FT /note="P->A: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:26476413"
FT MUTAGEN 138
FT /note="R->A: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:26476413"
FT MUTAGEN 167
FT /note="S->A: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:26476413"
FT MUTAGEN 171
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26476413"
FT MUTAGEN 206
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26476413"
SQ SEQUENCE 216 AA; 24360 MW; 77650A6E3E011FD4 CRC64;
MSAITIRAMT IGDYEEVEAF LAVHFFKQEP LMLIPQEDPK QSEVSSAEAE LHRSLIPQDL
SLVAVDGERI VGVVLAGELV PEDLEREYQE AEQKEITCLL DKIHKFLAGI ERQANIFKHY
GVERALYLYM LGVDVSIRRQ RVGTRLVEAT IELGRQRGFP VVTSTCSNQN SKRLMTALNM
ECILTKDYAD YKDEHGEIVL RASEPHTSAS VVAIRL
