Q9V9A7 · MCCB_DROME
- ProteinProbable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- GeneMccc2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids578 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism (By similarity).
Vital for adult survival
Vital for adult survival
Catalytic activity
- 3-methyl-(2E)-butenoyl-CoA + hydrogencarbonate + ATP = 3-methyl-(2E)-glutaconyl-CoA + ADP + phosphate + H+
Pathway
Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 3-methylcrotonyl-CoA carboxylase complex, mitochondrial | |
Cellular Component | methylcrotonoyl-CoA carboxylase complex | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | methylcrotonoyl-CoA carboxylase activity | |
Biological Process | coenzyme A metabolic process | |
Biological Process | L-leucine catabolic process | |
Biological Process | regulation of eclosion |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- EC number
- Short namesMCCase subunit beta
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9V9A7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-29 | Mitochondrion | ||||
Sequence: MIRLNWLFRSSSVLLRSQVRLLHVGDANV | ||||||
Chain | PRO_0000000297 | 30-578 | Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial | |||
Sequence: LHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPDKLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNSYNDQLMHSSQVNFQTATPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM |
Proteomic databases
Expression
Tissue specificity
Expressed in third instar larval ring gland (lateral and medial secretory cells and corpus cardiacum cells) and CNS.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 48-305 | CoA carboxyltransferase N-terminal | ||||
Sequence: MASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPDKLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNSYNDQL | ||||||
Region | 48-570 | Carboxyltransferase | ||||
Sequence: MASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPDKLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNSYNDQLMHSSQVNFQTATPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQE | ||||||
Domain | 321-570 | CoA carboxyltransferase C-terminal | ||||
Sequence: AVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQE | ||||||
Region | 355-388 | Acyl-CoA binding | ||||
Sequence: DGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNN |
Sequence similarities
Belongs to the AccD/PCCB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length578
- Mass (Da)62,648
- Last updated2000-05-01 v1
- ChecksumAF5E2ABBE36B18F0
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 50 | in Ref. 4; no nucleotide entry | ||||
Sequence: S → R | ||||||
Sequence conflict | 96 | in Ref. 4; no nucleotide entry | ||||
Sequence: F → G | ||||||
Sequence conflict | 274 | in Ref. 3; AAL89883 | ||||
Sequence: H → N | ||||||
Sequence conflict | 277 | in Ref. 4; no nucleotide entry | ||||
Sequence: L → V | ||||||
Sequence conflict | 330 | in Ref. 4; no nucleotide entry | ||||
Sequence: E → R | ||||||
Sequence conflict | 376-377 | in Ref. 4; no nucleotide entry | ||||
Sequence: KL → NV | ||||||
Sequence conflict | 422 | in Ref. 4; no nucleotide entry | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AAM70824.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF006654 EMBL· GenBank· DDBJ | AAB62570.1 EMBL· GenBank· DDBJ | mRNA | ||
AY084145 EMBL· GenBank· DDBJ | AAL89883.1 EMBL· GenBank· DDBJ | mRNA |