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Protein

Long-chain-fatty-acid--CoA ligase bubblegum-like

Gene

CG4500

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei491 – 4911ATPBy similarity
Binding sitei506 – 5061ATPBy similarity
Binding sitei639 – 6391ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi223 – 2319ATPBy similarity
Nucleotide bindingi414 – 4196ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • long-chain fatty acid metabolic process Source: UniProtKB
  • mesoderm development 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:
Long-chain-fatty-acid--CoA ligase bubblegum-like (EC:6.2.1.3)
Gene namesi
ORF Names:CG4500
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0028519. CG4500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681Long-chain-fatty-acid--CoA ligase bubblegum-likePRO_0000315818Add
BLAST

Proteomic databases

PaxDbiQ9V3U0.
PRIDEiQ9V3U0.

Expressioni

Gene expression databases

BgeeiQ9V3U0.
GenevisibleiQ9V3U0. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0080168.

Structurei

3D structure databases

ProteinModelPortaliQ9V3U0.
SMRiQ9V3U0. Positions 35-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
InParanoidiQ9V3U0.
OMAiWIVLPRD.
OrthoDBiEOG7B5WVB.
PhylomeDBiQ9V3U0.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9V3U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDLKPATSY RSTSLHDAVK LRLDEPSSFS QTVPPQTIPE FFKESCEKYS
60 70 80 90 100
DLPALVWETP GSGNDGWTTL TFGEYQERVE QAALMLLSVG VEERSSVGIL
110 120 130 140 150
AFNCPEWFFA EFGALRAGAV VAGVYPSNSA EAVHHVLATG ESSVCVVDDA
160 170 180 190 200
QQMAKLRAIK ERLPRLKAVI QLHGPFEAFV DHEPGYFSWQ KLQEQTFSSE
210 220 230 240 250
LKEELLARES RIRANECAML IFTSGTVGMP KAVMLSHDNL VFDTKSAAAH
260 270 280 290 300
MQDIQVGKES FVSYLPLSHV AAQIFDVFLG LSHAGCVTFA DKDALKGTLI
310 320 330 340 350
KTFRKARPTK MFGVPRVFEK LQERLVAAEA KARPYSRLLL ARARAAVAEH
360 370 380 390 400
QTTLMAGKSP SIYGNAKYWL ACRVVKPIRE MIGVDNCRVF FTGGAPTSEE
410 420 430 440 450
LKQFFLGLDI ALGECYGMSE TSGAITLNVD ISNLYSAGQA CEGVTLKIHE
460 470 480 490 500
PDCNGQGEIL MRGRLVFMGY LGLPDKTEET VKEDGWLHSG DLGYIDPKGN
510 520 530 540 550
LIISGRLKEL IITAGGENIP PVHIEELIKK ELPCVSNVLL IGDHRKYLTV
560 570 580 590 600
LLSLKTKCDA KTGIPLDALR EETIEWLRDL DIHETRLSEL LNIPADLQLP
610 620 630 640 650
NDTAALAATL EITAKPKLLE AIEEGIKRAN KYAISNAQKV QKFALIAHEF
660 670 680
SVATGELGPT LKIRRNIVHA KYAKVIERLY K
Length:681
Mass (Da):75,152
Last modified:May 1, 2000 - v1
Checksum:i6310902CC494712E
GO

Sequence cautioni

The sequence AAM12254.1 differs from that shown. Reason: Erroneous termination at position 195. Translated as Gln.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53370.1.
BT021247 mRNA. Translation: AAX33395.1.
AY095523 mRNA. Translation: AAM12254.1. Sequence problems.
RefSeqiNP_609696.1. NM_135852.4.
UniGeneiDm.11081.

Genome annotation databases

EnsemblMetazoaiFBtr0080591; FBpp0080168; FBgn0028519.
GeneIDi34822.
KEGGidme:Dmel_CG4500.
UCSCiCG4500-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53370.1.
BT021247 mRNA. Translation: AAX33395.1.
AY095523 mRNA. Translation: AAM12254.1. Sequence problems.
RefSeqiNP_609696.1. NM_135852.4.
UniGeneiDm.11081.

3D structure databases

ProteinModelPortaliQ9V3U0.
SMRiQ9V3U0. Positions 35-542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0080168.

Proteomic databases

PaxDbiQ9V3U0.
PRIDEiQ9V3U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080591; FBpp0080168; FBgn0028519.
GeneIDi34822.
KEGGidme:Dmel_CG4500.
UCSCiCG4500-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0028519. CG4500.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
InParanoidiQ9V3U0.
OMAiWIVLPRD.
OrthoDBiEOG7B5WVB.
PhylomeDBiQ9V3U0.

Miscellaneous databases

GenomeRNAii34822.
NextBioi790390.
PROiQ9V3U0.

Gene expression databases

BgeeiQ9V3U0.
GenevisibleiQ9V3U0. 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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-681.
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiBGML_DROME
AccessioniPrimary (citable) accession number: Q9V3U0
Secondary accession number(s): Q8SWR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 100 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.