FABD_DROME
ID FABD_DROME Reviewed; 379 AA.
AC Q8T3L6; B6IDQ4; Q9VVD5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable malonyl-CoA-acyl carrier protein transacylase, mitochondrial;
DE Short=MCT;
DE EC=2.3.1.39;
DE AltName: Full=Bad egg;
DE AltName: Full=[Acyl-carrier-protein] malonyltransferase;
DE Flags: Precursor;
GN Name=beg; ORFNames=CG7842;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18245854; DOI=10.1534/genetics.106.065912;
RA Khokhar A., Chen N., Yuan J.-P., Li Y., Landis G.N., Beaulieu G., Kaur H.,
RA Tower J.;
RT "Conditional switches for extracellular matrix patterning in Drosophila
RT melanogaster.";
RL Genetics 178:1283-1293(2008).
CC -!- FUNCTION: Catalyzes the transfer of a malonyl moiety from malonyl-CoA
CC to the free thiol group of the phosphopantetheine arm of the ACP
CC protein. This suggests the existence of the biosynthesis of fatty acids
CC in mitochondria (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Eggs have a thin shell.
CC {ECO:0000269|PubMed:18245854}.
CC -!- SIMILARITY: Belongs to the type II malonyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF49377.1; -; Genomic_DNA.
DR EMBL; AY094770; AAM11123.1; -; mRNA.
DR EMBL; BT050494; ACJ13201.1; -; mRNA.
DR RefSeq; NP_648950.1; NM_140693.3.
DR AlphaFoldDB; Q8T3L6; -.
DR SMR; Q8T3L6; -.
DR IntAct; Q8T3L6; 5.
DR STRING; 7227.FBpp0075038; -.
DR PaxDb; Q8T3L6; -.
DR PRIDE; Q8T3L6; -.
DR DNASU; 39910; -.
DR EnsemblMetazoa; FBtr0075278; FBpp0075038; FBgn0036691.
DR GeneID; 39910; -.
DR KEGG; dme:Dmel_CG7842; -.
DR UCSC; CG7842-RA; d. melanogaster.
DR CTD; 39910; -.
DR FlyBase; FBgn0036691; beg.
DR VEuPathDB; VectorBase:FBgn0036691; -.
DR eggNOG; KOG2926; Eukaryota.
DR GeneTree; ENSGT00390000013715; -.
DR HOGENOM; CLU_030558_2_1_1; -.
DR InParanoid; Q8T3L6; -.
DR OMA; AANYNCP; -.
DR OrthoDB; 1037268at2759; -.
DR PhylomeDB; Q8T3L6; -.
DR Reactome; R-DME-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 39910; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 39910; -.
DR PRO; PR:Q8T3L6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036691; Expressed in embryonic/larval hemocyte (Drosophila) and 21 other tissues.
DR Genevisible; Q8T3L6; DM.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004312; F:fatty acid synthase activity; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.366.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..379
FT /note="Probable malonyl-CoA-acyl carrier protein
FT transacylase, mitochondrial"
FT /id="PRO_0000000590"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT CONFLICT 61
FT /note="A -> T (in Ref. 3; AAM11123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42086 MW; DC9BCD8624C7B623 CRC64;
MLAARRLLRS PRITGALSWS RWSSDAAKAT TETSALLQNA EKRQQLLNEL SEPLEQKGRP
AIDPKETSVM LFPGQGTQYV GMAKDLLRFP GARRIFELAN EVLKYDLLKI CLEGPREKLN
RTEHAQLAVM VSSLAALEQL REERPKAIET CVAAAGFSLG EITALVYADA LPFDKALRLV
QVRATAMQAA CDQAAGAMAM TLYGPDTNLG EACARAQQWC LDKGVESPYC GIANYMYPHC
KVVAGNVEAL EFLEQNAKSF KIRRMKRLAV SGAFHTPLMQ SAVEPFTKAL KTVRLQDPVI
RVYSNVDGKP YRHAKHILTQ LPKQIVRPVK WEQTLHEMYE RKQGVDFPRT FECGPGKGLV
QVLEKVNAKA AQSSFNVIA
