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Q9V3S9 (BGM_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processFatty acid metabolism
Lipid metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 666666Very long-chain-fatty-acid--CoA ligase bubblegum
PRO_0000315817

Regions

Nucleotide binding229 – 2379ATP By similarity
Nucleotide binding417 – 4226ATP By similarity

Sites

Binding site4951ATP By similarity
Binding site5101ATP By similarity
Binding site6241ATP By similarity

Experimental info

Sequence conflict2121M → K in AAM48344. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9V3S9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6F437947FE6B922C

FASTA66673,611
        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

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_524698.1. NM_079959.3.
UniGeneDm.23376.

3D structure databases

ProteinModelPortalQ9V3S9.
SMRQ9V3S9. Positions 78-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0080167.

Proteomic databases

PaxDbQ9V3S9.
PRIDEQ9V3S9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080590; FBpp0080167; FBgn0027348.
GeneID44117.
KEGGdme:Dmel_CG4501.
UCSCCG4501-RA. d. melanogaster.

Organism-specific databases

CTD44117.
FlyBaseFBgn0027348. bgm.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000101725.
InParanoidQ9V3S9.
KOK15013.
OMALLTIKCQ.
OrthoDBEOG7B5WVB.
PhylomeDBQ9V3S9.

Gene expression databases

BgeeQ9V3S9.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACSBG1. drosophila.
GenomeRNAi44117.
NextBio836801.
PROQ9V3S9.

Entry information

Entry nameBGM_DROME
AccessionPrimary (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: February 19, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents