Q9V3S9 (BGM_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Very long-chain-fatty-acid--CoA ligase bubblegum
EC=6.2.1.-
EC=6.2.1.3

Gene names

Name:	bgm
ORF Names:	CG4501

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	666 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Mediates activation of very-long-chain fatty acids. Probably also able to mediate activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Ref.4
Catalytic activity	ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.4
Disruption phenotype	Adult neurodegeneration, with marked dilation of photoreceptor axons. Effects are probably due to elevated levels of very long chain fatty acids (VLCFAs). Feeding the fly mutant with glyceryl trioleate oil, blocks the accumulation of excess VLCFAs as well as development of the pathology. Ref.4
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from mutant phenotype Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 666	666	Very long-chain-fatty-acid--CoA ligase bubblegum		PRO_0000315817
Regions
	Nucleotide binding	229 – 237	9	ATP By similarity
	Nucleotide binding	417 – 422	6	ATP By similarity
Sites
	Binding site	495	1	ATP By similarity
	Binding site	510	1	ATP By similarity
	Binding site	624	1	ATP By similarity
Experimental info
	Sequence conflict	212	1	M → K in AAM48344. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9V3S9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6F437947FE6B922C	FASTA	666	73,611
	10 20 30 40 50 60 MSTIDALYNR PGPNRLRQAD AYRTTNRQDA VKIRMAKDGI GAEEPISVPG LLKRTVNNYG 70 80 90 100 110 120 DYPALRTKNG KNGYHTVTYK QYEQKVHQVA KAFIKLGLEE HHSVGVLAFN CAEWFYSAMG 130 140 150 160 170 180 AIHARGIIAG IYTTNSADAV QHVLESSHAQ IVVVDDAKQM DKIHAIRDKL PKLKAAIQIQ 190 200 210 220 230 240 EPYSPYLKKE DGYYRWSEIE SMNVSDVEDQ YMTRLENVAI NECCCLVYTS GTVGMPKGVM 250 260 270 280 290 300 LSHDNITFDV RGIVKAMDRV VVGAESIVSY LPLSHVAAQT VDIYTCAFVA GCIWFADKDA 310 320 330 340 350 360 LKGTLVKSLQ DARPTRFMGV PRVYEKFQER MVAVASSSGS LKKMLASWAK GITLKHYMVS 370 380 390 400 410 420 QGKSSGGFRY KIAKSLIMSK VKQALGFDRV LTLASAAAPM SPETKKYFLS LDLKIVDAFG 430 440 450 460 470 480 MSETAGCHTI CLPDSVGLNT IGKTLPGCES KFINKDANGH GELCIRGRHV FMGYIDNKEK 490 500 510 520 530 540 TEESLDDDCW LHSGDLGFVD DKGYVSLTGR SKEIIITAGG ENIPPVHIEN TIKKELDAIS 550 560 570 580 590 600 NAFLVGEQRK YLTVLITLKT EVDKDSGEPL DELSHESSVW VKSLGVEHKT VSDILAAGPC 610 620 630 640 650 660 PKVWKSIEDA IKRANKQSIS NAQKVQKFTI LPHDFSIPTG ELGPTLKVKR NVVSKMYADE IEKLYA

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]	"Preventing neurodegeneration in the Drosophila mutant bubblegum." Min K.-T., Benzer S. Science 284:1985-1988(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014134 Genomic DNA. Translation: AAF53368.1. AY118315 mRNA. Translation: AAM48344.1.
RefSeq	NP_524698.1. NM_079959.3.
UniGene	Dm.23376.
3D structure databases
ProteinModelPortal	Q9V3S9.
SMR	Q9V3S9. Positions 78-589.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0080167.
Proteomic databases
PaxDb	Q9V3S9.
PRIDE	Q9V3S9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0080590; FBpp0080167; FBgn0027348.
GeneID	44117.
KEGG	dme:Dmel_CG4501.
UCSC	CG4501-RA. d. melanogaster.
Organism-specific databases
CTD	44117.
FlyBase	FBgn0027348. bgm.
Phylogenomic databases
eggNOG	COG1022.
GeneTree	ENSGT00690000101725.
InParanoid	Q9V3S9.
KO	K15013.
OMA	LLTIKCQ.
OrthoDB	EOG7B5WVB.
PhylomeDB	Q9V3S9.
Gene expression databases
Bgee	Q9V3S9.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ACSBG1. drosophila.
GenomeRNAi	44117.
NextBio	836801.
PRO	Q9V3S9.

Entry information

Entry name

BGM_DROME

Accession

Primary (citable) accession number: Q9V3S9
Secondary accession number(s): Q8MT84

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 1, 2000
Last modified:	November 13, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project