Q8T3L6 (FABD_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable malonyl-CoA-acyl carrier protein transacylase, mitochondrial
Short name=MCT
EC=2.3.1.39

Alternative name(s):
Bad egg
[Acyl-carrier-protein] malonyltransferase

Gene names

Name:	beg
ORF Names:	CG7842

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the ACP protein. This suggests the existence of the biosynthesis of fatty acids in mitochondrias By similarity.
Catalytic activity	Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subcellular location	Mitochondrion Probable.
Disruption phenotype	Eggs have a thin shell. Ref.5
Sequence similarities	Belongs to the type II malonyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	[acyl-carrier-protein] S-malonyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion Potential
	Chain	24 – 379	356	Probable malonyl-CoA-acyl carrier protein transacylase, mitochondrial		PRO_0000000590
Sites
	Active site	158	1	By similarity
	Active site	275	1	By similarity
Experimental info
	Sequence conflict	61	1	A → T in AAM11123. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8T3L6 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: DC9BCD8624C7B623	FASTA	379	42,086
	10 20 30 40 50 60 MLAARRLLRS PRITGALSWS RWSSDAAKAT TETSALLQNA EKRQQLLNEL SEPLEQKGRP 70 80 90 100 110 120 AIDPKETSVM LFPGQGTQYV GMAKDLLRFP GARRIFELAN EVLKYDLLKI CLEGPREKLN 130 140 150 160 170 180 RTEHAQLAVM VSSLAALEQL REERPKAIET CVAAAGFSLG EITALVYADA LPFDKALRLV 190 200 210 220 230 240 QVRATAMQAA CDQAAGAMAM TLYGPDTNLG EACARAQQWC LDKGVESPYC GIANYMYPHC 250 260 270 280 290 300 KVVAGNVEAL EFLEQNAKSF KIRRMKRLAV SGAFHTPLMQ SAVEPFTKAL KTVRLQDPVI 310 320 330 340 350 360 RVYSNVDGKP YRHAKHILTQ LPKQIVRPVK WEQTLHEMYE RKQGVDFPRT FECGPGKGLV 370 QVLEKVNAKA AQSSFNVIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Ovary.
[4]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[5]	"Conditional switches for extracellular matrix patterning in Drosophila melanogaster." Khokhar A., Chen N., Yuan J.-P., Li Y., Landis G.N., Beaulieu G., Kaur H., Tower J. Genetics 178:1283-1293(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014296 Genomic DNA. Translation: AAF49377.1. AY094770 mRNA. Translation: AAM11123.1. BT050494 mRNA. Translation: ACJ13201.1.
RefSeq	NP_648950.1. NM_140693.3.
UniGene	Dm.12916.
3D structure databases
ProteinModelPortal	Q8T3L6.
SMR	Q8T3L6. Positions 66-373.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0075038.
Proteomic databases
PaxDb	Q8T3L6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0075278; FBpp0075038; FBgn0036691.
GeneID	39910.
KEGG	dme:Dmel_CG7842.
UCSC	CG7842-RA. d. melanogaster.
Organism-specific databases
CTD	39910.
FlyBase	FBgn0036691. beg.
Phylogenomic databases
eggNOG	COG0331.
GeneTree	ENSGT00390000013715.
InParanoid	Q8T3L6.
KO	K00645.
OMA	AFHTRFM.
OrthoDB	EOG4Q83D0.
PhylomeDB	Q8T3L6.
Enzyme and pathway databases
UniPathway	UPA00094.
Gene expression databases
Bgee	Q8T3L6.
GermOnline	CG7842. Drosophila melanogaster.
Family and domain databases
Gene3D	3.40.366.10. 2 hits.
InterPro	IPR001227. Ac_transferase_dom. IPR014043. Acyl_transferase. IPR016035. Acyl_Trfase/lysoPLipase. IPR016036. Malonyl_transacylase_ACP-bd. [Graphical view]
Pfam	PF00698. Acyl_transf_1. 1 hit. [Graphical view]
SUPFAM	SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	39910.
NextBio	816051.

Entry information

Entry name

FABD_DROME

Accession

Primary (citable) accession number: Q8T3L6
Secondary accession number(s): B6IDQ4, Q9VVD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project