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Reviewed, UniProtKB/Swiss-Prot Q9V9A7 (MCCB_DROME)

Last modified January 19, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
      Short name=MCCase subunit beta
    EC=6.4.1.4
Alternative name(s):
    3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
    3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
    3-methylcrotonyl-CoA carboxylase 2
Gene names
Name: L(2)04524
ORF Names: CG3267
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Vital for adult survival. Ref.3

Catalytic activity

ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.

Pathway

Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.

Subcellular location

Mitochondrion matrix By similarity UniProtKB P07633.

Tissue specificity

Expressed in third instar larval ring gland (lateral and medial secretory cells and corpus cardiacum cells) and CNS. Ref.3

Sequence similarities

Contains 1 carboxyltransferase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion By similarity UniProtKB P07633
Chain? – 578Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrialPRO_0000000297

Regions

Domain54 – 572519Carboxyltransferase
Region355 – 38834Acyl-CoA binding Potential

Experimental info

Sequence conflict501S → R Ref.3
Sequence conflict961F → G Ref.3
Sequence conflict2771L → V Ref.3
Sequence conflict3301E → R Ref.3
Sequence conflict376 – 3772KL → NV Ref.3
Sequence conflict4221Missing Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q9V9A7-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AF5E2ABBE36B18F0

FASTA57862,648
        10         20         30         40         50         60 
MIRLNWLFRS SSVLLRSQVR LLHVGDANVL HSEVDKQSAE YKENAREMAS LVGDLRNFTS 

        70         80         90        100        110        120 
QVLKGGGQKA IERHTSRGKL LARERINLLL DKGSPFLELS ALAGHELYGE EVVNSGGIVT 

       130        140        150        160        170        180 
GVGRVCGTEC LVVANDATVK GGSYYPITVK KHLRAQEIAQ ENRLPCIYLV DSGGANLPRQ 

       190        200        210        220        230        240 
ADVFPDKLHF GRIFYNQANM SAQGIPQIAV VMGSCTAGGA YVPAMADESI IVKKQGTIFL 

       250        260        270        280        290        300 
AGPPLVKAAT GEEVSAEDLG GADLHCKTSG VTDHYALDDE HALYLARQIV SNLNLSATNS 

       310        320        330        340        350        360 
YNDQLMHSSQ VNFQTATPPS AVEEPRYDAE ELYGIVGPNL TKSFDVREVI ARIVDGSRFT 

       370        380        390        400        410        420 
EFKKLYGETL VCGFAKLYGH TVGIVGNNGV LFSESALKGA HFIQLCAQRK IPLVFLQNIT 

       430        440        450        460        470        480 
GFMVGRDAEA NGIAKNGAKM VTAVACANVP KFTVIIGGSY GAGNYGMCGR AYSPRFLYMW 

       490        500        510        520        530        540 
PNSRISVMGG TQAANVMAQI TEDQRKRAGK EFSEEEAQKL KAPIVEMFEA EGSPYYSTAR 

       550        560        570 
LWDDGIIDPA NTRQILGLSL KAALNNAGQE TKFGVFRM

« Hide

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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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"Genes expressed in the ring gland, the major endocrine organ of Drosophila melanogaster."
Harvie P.D., Filippova M., Bryant P.J.
Genetics 149:217-231(1998) [PubMed: 9584098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 43-126 AND 271-578, TISSUE SPECIFICITY.
Tissue: Larval CNS and Larval ring gland.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013599 Genomic DNA. Translation: AAM70824.1.
AF006654 mRNA. Translation: AAB62570.1.
RefSeqNP_652724.1.
UniGeneDm.5216

3D structure databases

SMRQ9V9A7. Positions 45-576.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9V9A7.

Proteomic databases

PRIDEQ9V9A7.

Genome annotation databases

EnsemblFBtr0086126; FBpp0085460; FBgn0042083; Drosophila melanogaster. [Genome view]
GeneID59261.
KEGGdme:Dmel_CG3267.
NMPDRfig|7227.3.peg.3506.
UCSCCG3267-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0042083. CG3267.

Phylogenomic databases

InParanoidQ9V9A7.
OMAAYHGDSV.
OrthoDBEOG9B2T3K.
PhylomeDBQ9V9A7.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-003088-MONOMER.
BRENDA6.4.1.4. 48.

Gene expression databases

ArrayExpressQ9V9A7.
GermOnlineCG3267. Drosophila melanogaster.

Family and domain databases

InterProIPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PROSITEPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio841761.

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Entry information

Entry nameMCCB_DROME
AccessionPrimary (citable) accession number: Q9V9A7
Secondary accession number(s): O18364
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 2000
Last modified: January 19, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents