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UniProtKB/Swiss-Prot entry Q9VSA3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACADM_DROME
Primary accession number Q9VSA3
Secondary accession numbers None
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 66)
Name and origin of the protein
Protein name Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial [Precursor]
Synonyms MCAD
EC 1.3.99.3
Gene name
ORFNames: CG12262
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE014296; AAF50524.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY089546; AAL90284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_648149.1; -.
UniGene Dm.879
3D structure databases
HSSP P41367; 3MDE. [HSSP ENTRY / PDB]
SMR Q9VSA3; 32-409.
ModBase Q9VSA3.
Protein-protein interaction databases
DIP DIP:20518N; -.
IntAct Q9VSA3; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-015630-MON; -.
Organism-specific databases
FlyBase FBgn0035811; CG12262.
Gene expression databases
ArrayExpress Q9VSA3; -.
GermOnline CG12262; Drosophila melanogaster.
Ontologies
GO
GO:0005811; Cellular component: lipid particle (inferred from direct assay from FlyBase).
GO:0003995; Molecular function: acyl-CoA dehydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006635; Biological process: fatty acid beta-oxidation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006089; Acyl-CoA_DHase_CS.
IPR006092; Acyl-CoA_DHase_N.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.
Gene3D G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.
Pfam PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00072; ACYL_COA_DH_1; 1.
PS00073; ACYL_COA_DH_2; 1.
BLOCKS Q9VSA3.
Genome annotation databases
Ensembl CG12262; Drosophila melanogaster. [Contig view]
GeneID 38864; -.
KEGG dme:Dmel_CG12262; -.
NMPDR fig|7227.3.peg.8730; -.
Phylogenomic databases
HOGENOM Q9VSA3; -.
Other
ProtoNet Q9VSA3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    17  17     Mitochondrion (By similarity). 
CHAIN   18   419  402     Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial. PRO_0000000508
NP_BIND   154   163  10     FAD (By similarity). 
NP_BIND   187   189  3     FAD (By similarity). 
NP_BIND   302   304  3     FAD (By similarity). 
NP_BIND   312   313  2     FAD (By similarity). 
NP_BIND   370   374  5     FAD (By similarity). 
NP_BIND   399   401  3     FAD (By similarity). 
REGION   274   277  4     Substrate binding (By similarity). 
ACT_SITE   397   397        Proton acceptor (By similarity). 
BINDING   163   163        Substrate; via carbonyl oxygen (By similarity). 
BINDING   398   398        Substrate; via amide nitrogen (By similarity). 
Sequence information
Length: 419 AA [This is the length of the unprocessed precursor] Molecular weight: 45871 Da [This is the MW of the unprocessed precursor] CRC64: 0B1970302243C394 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAFLNKLAAP ALRQLVSQSR AYAAVSHVSP NGTSFALTED QLQLQELARK FTREEIIPVA 

        70         80         90        100        110        120 
AQYDKSGEYP WPIIKKAWEL GLMNNHIPAD IGGLDLDVFT TCLSAEELAY GCTGIMTALE 

       130        140        150        160        170        180 
ASGLGQTPVI LSGNKEQKKK YLGRLLEEPL VAAYCVTEPG AGSDVSGIKT RAEKKGDEWV 

       190        200        210        220        230        240 
INGQKMWITN GGVANWYFVL ARTNPDPKCP PSKAFTGFIV ERDSPGLTPG RKELNMGQRA 

       250        260        270        280        290        300 
SDTRGITFED VRVPKENVLI GEGAGFKIAM GTFDKTRPPV AAGAVGLAQR CLDEALKYAL 

       310        320        330        340        350        360 
ERKTFGVPIA YHQAVQFMLA DMAIGVETSR LAWRLSAWEI DQGRRNSYYA SIAKCHAADM 

       370        380        390        400        410 
ANKIASDAVQ IFGGNGFNSE YPVEKLMRDA KIYQIYEGTS QIQRLIISRN MYEAAKGQA 

Q9VSA3 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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