ID   Q9VQL6_DROME            Unreviewed;      2409 AA.
AC   Q9VQL6;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   04-NOV-2026, entry version 205.
DE   RecName: Full=Fatty acid synthase {ECO:0000256|ARBA:ARBA00018769};
DE            EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948};
DE            EC=1.3.1.39 {ECO:0000256|ARBA:ARBA00012004};
DE            EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191};
DE            EC=2.3.1.85 {ECO:0000256|ARBA:ARBA00012873};
DE            EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
GN   Name=FASN2 {ECO:0000313|EMBL:AAF51149.1,
GN   ECO:0000313|FlyBase:FBgn0042627};
GN   Synonyms=DM_7295849 {ECO:0000313|EMBL:AAF51149.1}, Dmel\CG3524
GN   {ECO:0000313|EMBL:AAF51149.1}, FAS {ECO:0000313|EMBL:AAF51149.1},
GN   FAS-mb {ECO:0000313|EMBL:AAF51149.1}, FAS2
GN   {ECO:0000313|EMBL:AAF51149.1}, FAS[CG3524]
GN   {ECO:0000313|EMBL:AAF51149.1}, FASN {ECO:0000313|EMBL:AAF51149.1},
GN   fasn {ECO:0000313|EMBL:AAF51149.1}, fasn2
GN   {ECO:0000313|EMBL:AAF51149.1}, FASN[CG3524]
GN   {ECO:0000313|EMBL:AAF51149.1}, mFAS {ECO:0000313|EMBL:AAF51149.1},
GN   v(2)k05816 {ECO:0000313|EMBL:AAF51149.1};
GN   ORFNames=CG3524 {ECO:0000313|EMBL:AAF51149.1,
GN   ECO:0000313|FlyBase:FBgn0042627}, Dmel_CG3524
GN   {ECO:0000313|EMBL:AAF51149.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|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., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L.,
RA   Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C.,
RA   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   [4] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [9] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [10] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [11] {ECO:0000313|EMBL:AAF51149.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
CC   -!- FUNCTION: Fatty acid synthetase is a multifunctional enzyme that
CC       catalyzes the de novo biosynthesis of long-chain saturated fatty acids
CC       starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This
CC       multifunctional protein contains 7 catalytic activities and a site for
CC       the binding of the prosthetic group 4'-phosphopantetheine of the acyl
CC       carrier protein ([ACP]) domain. {ECO:0000256|ARBA:ARBA00023442}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-[ACP] + NADPH + H(+) = butanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC         Evidence={ECO:0000256|ARBA:ARBA00047500};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC         Evidence={ECO:0000256|ARBA:ARBA00047500};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-decenoyl-[ACP] + NADPH + H(+) = decanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78467, ChEBI:CHEBI:78468;
CC         Evidence={ECO:0000256|ARBA:ARBA00049521};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC         Evidence={ECO:0000256|ARBA:ARBA00049521};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-dodecenoyl-[ACP] + NADPH + H(+) = dodecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-
CC         COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000256|ARBA:ARBA00048281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC         Evidence={ECO:0000256|ARBA:ARBA00048281};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexadecenoyl-[ACP] + NADPH + H(+) = hexadecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-
CC         COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78481, ChEBI:CHEBI:78483;
CC         Evidence={ECO:0000256|ARBA:ARBA00047810};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC         Evidence={ECO:0000256|ARBA:ARBA00047810};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexenoyl-[ACP] + NADPH + H(+) = hexanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78458, ChEBI:CHEBI:78459;
CC         Evidence={ECO:0000256|ARBA:ARBA00047897};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC         Evidence={ECO:0000256|ARBA:ARBA00047897};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octadecenoyl-[ACP] + NADPH + H(+) = octadecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-
CC         COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78489, ChEBI:CHEBI:78495;
CC         Evidence={ECO:0000256|ARBA:ARBA00049019};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929;
CC         Evidence={ECO:0000256|ARBA:ARBA00049019};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octenoyl-[ACP] + NADPH + H(+) = octanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78462, ChEBI:CHEBI:78463;
CC         Evidence={ECO:0000256|ARBA:ARBA00048420};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC         Evidence={ECO:0000256|ARBA:ARBA00048420};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-tetradecenoyl-[ACP] + NADPH + H(+) = tetradecanoyl-[ACP]
CC         + NADP(+); Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-
CC         COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78475, ChEBI:CHEBI:78477;
CC         Evidence={ECO:0000256|ARBA:ARBA00049171};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC         Evidence={ECO:0000256|ARBA:ARBA00049171};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC         Evidence={ECO:0000256|ARBA:ARBA00023402};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC         Evidence={ECO:0000256|ARBA:ARBA00023402};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC         Evidence={ECO:0000256|ARBA:ARBA00023388};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC         Evidence={ECO:0000256|ARBA:ARBA00023388};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000256|ARBA:ARBA00023351};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC         Evidence={ECO:0000256|ARBA:ARBA00023351};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC         Evidence={ECO:0000256|ARBA:ARBA00023401};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC         Evidence={ECO:0000256|ARBA:ARBA00023401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC         Evidence={ECO:0000256|ARBA:ARBA00023373};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC         Evidence={ECO:0000256|ARBA:ARBA00023373};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489;
CC         Evidence={ECO:0000256|ARBA:ARBA00023399};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925;
CC         Evidence={ECO:0000256|ARBA:ARBA00023399};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC         Evidence={ECO:0000256|ARBA:ARBA00023332};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC         Evidence={ECO:0000256|ARBA:ARBA00023332};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC         Evidence={ECO:0000256|ARBA:ARBA00023398};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC         Evidence={ECO:0000256|ARBA:ARBA00023398};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxobutanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxybutanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625,
CC         Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451;
CC         Evidence={ECO:0000256|ARBA:ARBA00047953};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC         Evidence={ECO:0000256|ARBA:ARBA00047953};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxodecanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxydecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637,
CC         Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466;
CC         Evidence={ECO:0000256|ARBA:ARBA00047440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC         Evidence={ECO:0000256|ARBA:ARBA00047440};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxododecanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxydodecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641,
CC         Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470;
CC         Evidence={ECO:0000256|ARBA:ARBA00049263};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873;
CC         Evidence={ECO:0000256|ARBA:ARBA00049263};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexadecanoyl-[ACP] + NADPH + H(+) = (3R)-
CC         hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-
CC         COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480;
CC         Evidence={ECO:0000256|ARBA:ARBA00049414};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC         Evidence={ECO:0000256|ARBA:ARBA00049414};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxyhexanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629,
CC         Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457;
CC         Evidence={ECO:0000256|ARBA:ARBA00048571};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC         Evidence={ECO:0000256|ARBA:ARBA00048571};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctadecanoyl-[ACP] + NADPH + H(+) = (3R)-
CC         hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-
CC         COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488;
CC         Evidence={ECO:0000256|ARBA:ARBA00047300};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921;
CC         Evidence={ECO:0000256|ARBA:ARBA00047300};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxyoctanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633,
CC         Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461;
CC         Evidence={ECO:0000256|ARBA:ARBA00049422};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC         Evidence={ECO:0000256|ARBA:ARBA00049422};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxotetradecanoyl-[ACP] + NADPH + H(+) = (3R)-
CC         hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888,
CC         Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473,
CC         ChEBI:CHEBI:78474; Evidence={ECO:0000256|ARBA:ARBA00048935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889;
CC         Evidence={ECO:0000256|ARBA:ARBA00048935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH
CC         + H(+); Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000256|ARBA:ARBA00047400};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC         Evidence={ECO:0000256|ARBA:ARBA00047400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000256|ARBA:ARBA00023394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC         Evidence={ECO:0000256|ARBA:ARBA00023394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC         NADPH + H(+); Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00048650};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC         Evidence={ECO:0000256|ARBA:ARBA00048650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP]
CC         + holo-[ACP] + CO2; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00048506};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000256|ARBA:ARBA00048506};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H(+) = a long-chain
CC         fatty acid + (n+1) CoA + n CO2 + 2n NADP(+).; EC=2.3.1.85;
CC         Evidence={ECO:0000256|ARBA:ARBA00044883};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxobutanoyl-[ACP] +
CC         holo-[ACP] + CO2; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC         Evidence={ECO:0000256|ARBA:ARBA00047961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801;
CC         Evidence={ECO:0000256|ARBA:ARBA00047961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxohexanoyl-[ACP] +
CC         holo-[ACP] + CO2; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC         Evidence={ECO:0000256|ARBA:ARBA00049449};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC         Evidence={ECO:0000256|ARBA:ARBA00049449};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxododecanoyl-[ACP]
CC         + holo-[ACP] + CO2; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC         Evidence={ECO:0000256|ARBA:ARBA00049109};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC         Evidence={ECO:0000256|ARBA:ARBA00049109};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxotetradecanoyl-
CC         [ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC         Evidence={ECO:0000256|ARBA:ARBA00047578};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC         Evidence={ECO:0000256|ARBA:ARBA00047578};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-[ACP] + H2O = hexadecanoate + holo-[ACP] + H(+);
CC         Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00048704};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC         Evidence={ECO:0000256|ARBA:ARBA00048704};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctadecanoyl-
CC         [ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487;
CC         Evidence={ECO:0000256|ARBA:ARBA00048051};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917;
CC         Evidence={ECO:0000256|ARBA:ARBA00048051};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctanoyl-[ACP] +
CC         holo-[ACP] + CO2; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC         Evidence={ECO:0000256|ARBA:ARBA00047394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC         Evidence={ECO:0000256|ARBA:ARBA00047394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA;
CC         Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446; EC=2.3.1.38;
CC         Evidence={ECO:0000256|ARBA:ARBA00048691};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789;
CC         Evidence={ECO:0000256|ARBA:ARBA00048691};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=octanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxodecanoyl-[ACP] +
CC         holo-[ACP] + CO2; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC         Evidence={ECO:0000256|ARBA:ARBA00049533};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC         Evidence={ECO:0000256|ARBA:ARBA00049533};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tetradecanoyl-[ACP] + H2O = tetradecanoate + holo-[ACP] +
CC         H(+); Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00048289};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC         Evidence={ECO:0000256|ARBA:ARBA00048289};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tetradecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-
CC         oxohexadecanoyl-[ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:41900,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC         ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00047451};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC         Evidence={ECO:0000256|ARBA:ARBA00047451};
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00258};
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DR   EMBL; AE014134; AAF51149.1; -; Genomic_DNA.
DR   RefSeq; NP_647613.1; NM_139356.2.
DR   SMR; Q9VQL6; -.
DR   IntAct; Q9VQL6; 8.
DR   ESTHER; drome-CG3524; Thioesterase.
DR   GeneID; 117361; -.
DR   UCSC; CG3524-RA; d. melanogaster.
DR   AGR; FB:FBgn0042627; -.
DR   CTD; 100000781; -.
DR   FlyBase; FBgn0042627; FASN2.
DR   VEuPathDB; VectorBase:FBgn0042627; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_7_1; -.
DR   OrthoDB; 329835at2759; -.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 117361; 0 hits in 1 CRISPR screen.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0042627; Expressed in adult oenocyte (Drosophila) in dorsal vessel heart and 58 other cell types or tissues.
DR   GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0141148; F:enoyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004312; F:fatty acid synthase activity; IMP:FlyBase.
DR   GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:FlyBase.
DR   GO; GO:0006723; P:cuticle hydrocarbon biosynthetic process; IMP:FlyBase.
DR   GO; GO:1902321; P:methyl-branched fatty acid biosynthetic process; IMP:FlyBase.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   FunFam; 1.10.1200.10:FF:000013; Fatty acid synthase; 1.
DR   FunFam; 3.40.50.1820:FF:000059; Fatty acid synthase; 1.
DR   FunFam; 3.90.180.10:FF:000015; Fatty acid synthase; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase_dom.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR020843; ER.
DR   InterPro; IPR049391; FAS_pseudo-KR.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR014031; KAS_C.
DR   InterPro; IPR014030; KAS_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR057326; KR_dom.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR049900; PKS_mFAS_DH.
DR   InterPro; IPR050091; PKS_NRPS_Biosynth_Enz.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Acyltransferase {ECO:0000313|EMBL:AAF51149.1};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAF51149.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450, ECO:0000256|PROSITE-
KW   ProRule:PRU00258}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9VQL6};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAF51149.1}.
FT   DOMAIN          16..425
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          863..1126
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000259|PROSITE:PS52019"
FT   DOMAIN          2025..2102
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          863..987
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01363"
FT   REGION          1000..1126
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        898
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1049
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01363"
FT   MOD_RES         2060
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2409 AA;  265872 MW;  2EF5E700057AC734 CRC64;
     MPSRKKAQGE SAAGEDADIV ISGLSGKLPE SSNIEEFKYN LLNGIDMVTD EPRRWEAGIY
     GLPERMAKMK DSDLEKFDDK FFSVHQKQAE LMDPCMRMLL ELTHEAIIDA GINPVQLRGS
     RTGVYIGLSF VETEHEIPNM EPSSINGYCL TGCARAMFAN RISYTFDFKG PSFIVDTACS
     SSLVALNHAF ADMRAGRCDY ALVAGVNLIL KPIFALQFLR LGIVSHDGSC KTFDAAANGY
     ARADTCAVVL LQRRKEAKRV YASILNVRTN TDGFKEQGVT FPDGRMQQAL LEETYSEIGL
     NPDEVVYVEA HGSGTPVGDD QEANMLSNFF CRPSRSTPLL IGSVKSNMGH AEPASGVSAL
     AKMIIAMEEG IIPKNLHYRT PNPSVPALVE GKLKVVDRNL PWQGGIVGLN SFGFGGANAH
     VVLKSHTKAK EPKACPKAGE AEQSLSLVTC SGRTEDAVNQ LLKVATEQRH DQELLTLIND
     IHSHPIPLHP FRGYAVLGTS GCVKEEVLPY EEEERPIWFV YAGMGSQWAR MAKDLMQLEV
     FRNSIQHCAE VLAQVDFDLI DVLTRSTERT FDNMLYSFVS VSAVQVALTD LLRVLDIRPD
     GIIGHSAGEL GAAYMDGCLT AEQTVLAAYW RGRSVLDTPD LPRGKMAAVG LSWEQIGSQI
     PKDCYPVCHN SDDNCTVSGP PSSMDAMIED LTAKGIFVRE VGSGGYAFHS PYIEGAAPML
     RRSLERLITE PKKKSIRWLS TSVKEAEWDS EKNHLASAGY FINNLISPVL FHQAVKRIPQ
     NALIVEIAPH GLFRAILRSL SPQISYVSLM QRGHANNFEF LLSQLGRLYA AGGQPQILKI
     SPSIPYPVSR GTPMLGSLVG WDHTQKWNYP KFKGGRQAGQ LSVELDLGKE ENVYLAGHTI
     DGRVLFPATG YMTLAWMSLA QQQGLDYLRT PVLFEDVVFH RATILSVGTV VKLTLNFFPG
     SSSFEICEGT SLVTSGKIRL VSNVQQEQLQ LSSLPGIAGS NKLSTKDIYK ELRLRGYDYT
     GVFQGILESD ISAVTGQLQW ADNWISFMDT MLQFRILSND IRELYVPTGI ERALIDPLKH
     LELAKKHQQK LTVNWHRNIS VVKCGGVEIH KMKTAQTQRR SGGQSPPSLE RYRFWPHSQH
     LGQREEQEKS RSTALAVAIQ LIIENSGGAV KLKGVELAGS RSTLDALSAV QLLELIEREP
     ILVGDMAVVT SSSNESELGE QLKEHGIRVI VKDIKAGAVE QQCHFVYSVN MLAQNSVKDL
     QHCLDSLKSD SGFLLLEEAA SRYNIIGKEK LNKLKLVSVL EQFFGTDRVL VLVRKLSKVQ
     SSQALTLHLT NKQFKWVNEL KNSIAKAQAE EKNLYLVAQG EPNSGALGLM NCLKREAGGH
     FLRLYLILDE GVPQFSLDDP FYAAQLAKDL VVNVYRNGSW GSYRHLKMES RPPMLPVEQA
     YVNTLVKGDL SSLRWIESPR SSPIQSQLEP CTVYYAPLNF RDVMLASGKL GVDALPGDLA
     YQDCVLGLEF AGRDSCGRRV MAMVTAKSLA TNCLANRNLL WEVPSKWTME QASTVPCVYA
     TVYYALVVRG QMKEGERILI HAGSGGVGQA AISVALAHGL TVFTTVGSKE KREFLLKRFP
     KLKAKNIGNS RDTSFEQLIM SETHGNGVEL VLNSLSEEKL QASIRCLALN GRFLEIGKFD
     LSNNTPLGMS VFLKNTSFHG ILLDSVMEGE EEMQLMVAKL VAEGIKSGAV QPLPTTVFAE
     QEIEKAFRFM ASGKHIGKVV IKVRLEEEQQ AALPRLRQIQ AIPRSYMHPE KSYILVGGLG
     GFGLELANWL VSRGARFLVL SSRSGVKSGY QALMIRRWHD RGVQVQIDTN DVTTAVGCQR
     LLEVSNKLAL VGGIFNLAAV LRDGLIEDQS PKNFEKVSAP KLLATIHLDK ISREICPALE
     YFVCFSSLSC GRGNMGQTNY GLANSTMERI CEQRQEYGYP GTAIQWGAIG DTGLIIEHMG
     NNETVVGGTL PQRMISCLET LDLFLQQPHP VMASMVVAEK RKTEQANRLS LIATIANIMG
     LRDVKSVSDK TTLFDLGMDS LMSTEIKQTL ERHFDLVLSA QEIRQLTFSA LRQIDAQEPP
     SASVSSPSAS STLSRIKEEA CVEVQPQSDE TRKVFAKEVL PQEVMVRLRS KAPVASEDPA
     VFFLAPIEGF TIAVEALAAS LTCPAYGLQC TEQVPLDSIE ACAAYYLRQI QKLQPLGPYH
     IVGYSYGCLL AHAIAVALEQ RRFGVKVIML DGAPTMASGY VQEAKKQTDD LNRQQSMTLA
     YFGALLADVD YNQLLQLLDG VQTWPSKLDK LADTLAGYTQ QTREVIKKAA CMFKQKLLLS
     ESYKGAKQLH SDVVLIKSAE HNAIMAQDYG LKEICSAQID MHVVEGTHRT FLKEPHTLQI
     IERVLRKRP
//