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Information on EC 6.4.1.4 - methylcrotonoyl-CoA carboxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q42523

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EC Tree
IUBMB Comments
A biotinyl-protein.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q42523
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mccc, 3-methylcrotonyl-coa carboxylase, mccase, methylcrotonyl-coa carboxylase, mcase, beta-methylcrotonyl-coa carboxylase, 3-mcc, 3-methylcrotonyl-coenzyme a carboxylase, 3-methylcrotonyl coa carboxylase, beta-methylcrotonyl coa carboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-methylcrotonyl-CoA carboxylase
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3-methylcrotonyl-CoA:carbon-dioxide ligase (ADP-forming)
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3-methylcrotonyl-coenzyme A carboxylase
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beta-methylcrotonyl CoA carboxylase
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beta-Methylcrotonyl coenzyme A carboxylase
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Carboxylase, methylcrotonyl coenzyme A
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Mcase
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MCCA
gene name for MCCA subunit of MCCAase
MCCase
MCCB
gene name for MCCB subunit of MCCAase
Methylcrotonyl coenzyme A carboxylase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-95-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-methylcrotonoyl-CoA + HCO3-
ADP + phosphate + 3-methylglutaconyl-CoA
show the reaction diagram
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-
-
?
ATP + 3-methylcrotonyl-CoA + HCO3-
ADP + phosphate + 3-methylglutaconyl-CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 3-methylcrotonyl-CoA + HCO3-
ADP + phosphate + 3-methylglutaconyl-CoA
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
T-DNA and transposon-tagged mutant alleles of the MCCA and MCCB genes of Arabidopsis thaliana are recovered. Mutations in either MCCA or MCCB block mitochondrial Leu catabolism. Under light deprivation conditions, the hyper-accumulation of Leu, 3-methylcrotonyl CoA and isovaleryl CoA indicates that mitochondrial and peroxisomal Leu catabolism pathways are independently regulated. Block in mitochondrial Leu catabolism is associated with an impaired reproductive growth phenotype. The decreased seed germination phenotype is only observed for homozygous mutant seeds
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MCCA_ARATH
734
0
80451
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 85000 + x * 60000, heteromeric enzyme composed of biotin-containing MCC-A and non-biotin-containing MCC-B subunits
85000
x * 85000 + x * 60000, heteromeric enzyme composed of biotin-containing MCC-A and non-biotin-containing MCC-B subunits
900000
nondenaturing PAGE, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polymer
x * 85000 + x * 60000, heteromeric enzyme composed of biotin-containing MCC-A and non-biotin-containing MCC-B subunits
additional information
heteromeric enzyme composed of 2 kinds of subunits, biotinylated MCC-A and non-, biotinylated MCC-B
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures diffracted to 1.5 A resolution of the Pseudomonas aeruginosa MCC (PaMCC) holoenzyme are shown, alone and in complex with coenzyme A. The structures show that the architecture and overall shape of PaMCC are strikingly different when compared to propionyl-CoA carboxylase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
MCCase is of significance in comprehending how the mevalonate shunt can divert carbon away from the biosynthesis of isoprenoids, such as cholesterol, which has major implications in the prevention of vascular degenerate diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weaver, L.M.; Lebrun, L.; Franklin, A.; Huang, L.; Hoffman, N.; Wurtele, E.S.; Nikolau, B.J.
Molecular cloning of the biotinylated subunit of 3-methylcrotonyl-coenzyme A carboxylase of Arabidopsis thaliana
Plant Physiol.
107
1013-1014
1995
Arabidopsis thaliana
Manually annotated by BRENDA team
McKean, A.L.; Ke, J.; Song, J.; Che, P.; Achenbach, S.; Nikolau, B.J.; Wurtele, E.S.
Molecular characterization of the non-biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase
J. Biol. Chem.
275
5582-5590
2000
Arabidopsis thaliana (Q9LDD8)
Manually annotated by BRENDA team
Che, P.; Wurtele, E.S.; Nikolau, B.J.
Metabolic and environmental regulation of 3-methylcrotonyl-coenzyme A carboxylase expression in Arabidopsis
Plant Physiol.
129
625-637
2002
Arabidopsis thaliana (Q42523)
Manually annotated by BRENDA team
Ding, G.; Che, P.; Ilarslan, H.; Wurtele, E.S.; Nikolau, B.J.
Genetic dissection of methylcrotonyl CoA carboxylase indicates a complex role for mitochondrial leucine catabolism during seed development and germination
Plant J.
70
562-577
2012
Arabidopsis thaliana (Q42523), Arabidopsis thaliana (Q9LDD8)
Manually annotated by BRENDA team