Information on EC 4.3.99.2 - carboxybiotin decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.3.99.2
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RECOMMENDED NAME
GeneOntology No.
carboxybiotin decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a carboxybiotinyl-[protein] + n Na+/in + H+/out = CO2 + a biotinyl-[protein] + n Na+/out (n: 1-2)
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
malonate degradation II (biotin-dependent)
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SYSTEMATIC NAME
IUBMB Comments
carboxybiotinyl-[protein] carboxy-lyase
The integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The free energy of the decarboxylation reaction is used to pump Na+ out of the cell. The enzyme is a member of the Na+-translocating decarboxylase family, other members of which include EC 4.1.1.3 (oxaloacetate decarboxylase) and EC 4.1.1.41 (methylmalonyl-CoA decarboxylase) [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
carboxybiotin decarboxylase is part of the methylmalonyl-CoA decarboxylase
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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carboxybiotin is cleaved at the membrane-bound subunit MadB of malonate decarboxylase Na+ pump with concomitant generation of a transmembrane Na+ gradient
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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carboxybiotin is cleaved at the membrane-bound subunit MadB of malonate decarboxylase Na+ pump with concomitant generation of a transmembrane Na+ gradient
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41200
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x * 41200, calculated
43023
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x * 43023, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methymalonyl-CoA decarboxylase complex
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recombinant isoform MadF. Despite coexpression of biotin ligase birA, MadF is poorly biotinylated. Existence of a biotin ligase in Malonomonas rubra with an altered substrate specificity different from that of BirA
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression with biotin ligase birA in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D149E
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mutation within putative membrane-spanning domains of the beta-subunit. Mutant retains oxaloacetate decarboxylase and Na+ transport activities
D149Q
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mutation within putative membrane-spanning domains of the beta-subunit. Mutant retains oxaloacetate decarboxylase and Na+ transport activities
D203E
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loss of oxaloacetate decarboxylase and Na+ transport activities, mutant retains the ability to form the carboxybiotin enzyme
D203N
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loss of oxaloacetate decarboxylase and Na+ transport activities, mutant retains the ability to form the carboxybiotin enzyme