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Protein

Very long-chain-fatty-acid--CoA ligase bubblegum

Gene

bgm

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei495 – 4951ATPBy similarity
Binding sitei510 – 5101ATPBy similarity
Binding sitei624 – 6241ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi229 – 2379ATPBy similarity
Nucleotide bindingi417 – 4226ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  • long-chain fatty acid metabolic process Source: UniProtKB
  • response to endoplasmic reticulum stress Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Very long-chain-fatty-acid--CoA ligase bubblegum (EC:6.2.1.-, EC:6.2.1.3)
Gene namesi
Name:bgm
ORF Names:CG4501
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0027348. bgm.

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 666666Very long-chain-fatty-acid--CoA ligase bubblegumPRO_0000315817Add
BLAST

Proteomic databases

PaxDbiQ9V3S9.
PRIDEiQ9V3S9.

Expressioni

Gene expression databases

BgeeiQ9V3S9.
ExpressionAtlasiQ9V3S9. differential.
GenevisibleiQ9V3S9. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0080167.

Structurei

3D structure databases

ProteinModelPortaliQ9V3S9.
SMRiQ9V3S9. Positions 78-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
InParanoidiQ9V3S9.
KOiK15013.
OMAiAINECCC.
OrthoDBiEOG7B5WVB.
PhylomeDBiQ9V3S9.

Family and domain databases

InterProiIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V3S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTIDALYNR PGPNRLRQAD AYRTTNRQDA VKIRMAKDGI GAEEPISVPG
60 70 80 90 100
LLKRTVNNYG DYPALRTKNG KNGYHTVTYK QYEQKVHQVA KAFIKLGLEE
110 120 130 140 150
HHSVGVLAFN CAEWFYSAMG AIHARGIIAG IYTTNSADAV QHVLESSHAQ
160 170 180 190 200
IVVVDDAKQM DKIHAIRDKL PKLKAAIQIQ EPYSPYLKKE DGYYRWSEIE
210 220 230 240 250
SMNVSDVEDQ YMTRLENVAI NECCCLVYTS GTVGMPKGVM LSHDNITFDV
260 270 280 290 300
RGIVKAMDRV VVGAESIVSY LPLSHVAAQT VDIYTCAFVA GCIWFADKDA
310 320 330 340 350
LKGTLVKSLQ DARPTRFMGV PRVYEKFQER MVAVASSSGS LKKMLASWAK
360 370 380 390 400
GITLKHYMVS QGKSSGGFRY KIAKSLIMSK VKQALGFDRV LTLASAAAPM
410 420 430 440 450
SPETKKYFLS LDLKIVDAFG MSETAGCHTI CLPDSVGLNT IGKTLPGCES
460 470 480 490 500
KFINKDANGH GELCIRGRHV FMGYIDNKEK TEESLDDDCW LHSGDLGFVD
510 520 530 540 550
DKGYVSLTGR SKEIIITAGG ENIPPVHIEN TIKKELDAIS NAFLVGEQRK
560 570 580 590 600
YLTVLITLKT EVDKDSGEPL DELSHESSVW VKSLGVEHKT VSDILAAGPC
610 620 630 640 650
PKVWKSIEDA IKRANKQSIS NAQKVQKFTI LPHDFSIPTG ELGPTLKVKR
660
NVVSKMYADE IEKLYA
Length:666
Mass (Da):73,611
Last modified:May 1, 2000 - v1
Checksum:i6F437947FE6B922C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121M → K in AAM48344 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53368.1.
AY118315 mRNA. Translation: AAM48344.1.
RefSeqiNP_001285923.1. NM_001298994.1.
NP_524698.1. NM_079959.4.
UniGeneiDm.23376.

Genome annotation databases

EnsemblMetazoaiFBtr0080590; FBpp0080167; FBgn0027348.
FBtr0346624; FBpp0312204; FBgn0027348.
GeneIDi44117.
KEGGidme:Dmel_CG4501.
UCSCiCG4501-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53368.1.
AY118315 mRNA. Translation: AAM48344.1.
RefSeqiNP_001285923.1. NM_001298994.1.
NP_524698.1. NM_079959.4.
UniGeneiDm.23376.

3D structure databases

ProteinModelPortaliQ9V3S9.
SMRiQ9V3S9. Positions 78-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0080167.

Proteomic databases

PaxDbiQ9V3S9.
PRIDEiQ9V3S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080590; FBpp0080167; FBgn0027348.
FBtr0346624; FBpp0312204; FBgn0027348.
GeneIDi44117.
KEGGidme:Dmel_CG4501.
UCSCiCG4501-RA. d. melanogaster.

Organism-specific databases

CTDi44117.
FlyBaseiFBgn0027348. bgm.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
InParanoidiQ9V3S9.
KOiK15013.
OMAiAINECCC.
OrthoDBiEOG7B5WVB.
PhylomeDBiQ9V3S9.

Miscellaneous databases

GenomeRNAii44117.
NextBioi836801.
PROiQ9V3S9.

Gene expression databases

BgeeiQ9V3S9.
ExpressionAtlasiQ9V3S9. differential.
GenevisibleiQ9V3S9. DM.

Family and domain databases

InterProiIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiBGM_DROME
AccessioniPrimary (citable) accession number: Q9V3S9
Secondary accession number(s): Q8MT84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.