Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | membrane-bound oxaloacetate decarboxylase complex, the alpha-subunit is a peripheral membrane protein on the cytosolic side of the membrane, where it associates with beta- and gamma-subunits that are embedded in the membrane. The beta-subunit is an integral membrane protein with nine transmembrane segments. The small gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus | Klebsiella aerogenes | 16020 | - |
membrane | membrane-bound oxaloacetate decarboxylase complex, the alpha-subunit is a peripheral membrane protein on the cytosolic side of the membrane, where it associates with beta- and gamma-subunits that are embedded in the membrane. The beta-subunit is an integral membrane protein with nine transmembrane segments. The small gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus | Vibrio cholerae serotype O1 | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus | Klebsiella aerogenes | |
Zn2+ | bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus | Vibrio cholerae serotype O1 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Klebsiella aerogenes | decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview | ? | - |
? | |
additional information | Vibrio cholerae serotype O1 | decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview | ? | - |
? | |
Oxaloacetate | Klebsiella aerogenes | - |
Pyruvate + CO2 | - |
? | |
Oxaloacetate | Vibrio cholerae serotype O1 | - |
Pyruvate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella aerogenes | - |
- |
- |
Vibrio cholerae serotype O1 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
oxaloacetate = pyruvate + CO2 | catalytic mechanism, overview. Carboxybiotin transits to the membrane-bound beta-subunit where it is decarboxylated to biotin and CO2 in a reaction that consumes a periplasmic proton and is coupled to Na+ translocation from the cytoplasm to the periplasm. The reaction is initiated by the enzyme-catalyzed decarboxylation of oxaloacetate in the carboxyltransferase domain of the alpha-subunit, yielding pyruvate and carboxybiotin. Subsequently, the C-terminal biotin carboxyl carrier protein domain on the alpha-subunit translocates to the beta-subunit where its decarboxylation is coupled to Na+ translocation. The OADC pump is reversible: at high concentrations of extracellular Na+, the pump will couple the downhill movement of Na+ into the cytosol with the carboxylation of pyruvate, to form oxaloacetate | Klebsiella aerogenes | |
oxaloacetate = pyruvate + CO2 | catalytic mechanism, overview. Carboxybiotin transits to the membrane-bound beta-subunit where it is decarboxylated to biotin and CO2 in a reaction that consumes a periplasmic proton and is coupled to Na+ translocation from the cytoplasm to the periplasm. The reaction is initiated by the enzyme-catalyzed decarboxylation of oxaloacetate in the carboxyltransferase domain of the alpha-subunit, yielding pyruvate and carboxybiotin. Subsequently, the C-terminal biotin carboxyl carrier protein domain on the alpha-subunit translocates to the beta-subunit where its decarboxylation is coupled to Na+ translocation. The OADC pump is reversible: at high concentrations of extracellular Na+, the pump will couple the downhill movement of Na+ into the cytosol with the carboxylation of pyruvate, to form oxaloacetate | Vibrio cholerae serotype O1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview | Klebsiella aerogenes | ? | - |
? | |
additional information | decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview | Vibrio cholerae serotype O1 | ? | - |
? | |
Oxaloacetate | - |
Klebsiella aerogenes | Pyruvate + CO2 | - |
? | |
Oxaloacetate | - |
Vibrio cholerae serotype O1 | Pyruvate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | in the absence of beta- or alpha-subunits, the gamma-subunit forms a homodimer through a dimerization interface in the carboxyltransferase domain | Klebsiella aerogenes |
tetramer | the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place | Klebsiella aerogenes |
tetramer | the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The about 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The about 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. the site of interaction with the gamma-subunit in Vibrio cholerae OADC is located in an intervening region between the carboxyltransferase and biotin carboxyl carrier protein domains of the alpha-subunit, termed the association domain. Tetramerization of alpha-OADC is mediated by an interaction between the association domain of the alpha-subunit and the cytosolic portion of the gamma-subunit in a manner. A biotin binding pocket, termed the exo-binding site, is located at the interface between the association domain and the carboxyltransferase domain. The interaction is facilitated by the tetramerization of alpha-OADC through interactions between the association domain and the the cytosolic portion of the gamma-subunit, which maintain two of the four alpha-OADC molecules in close proximity to the membrane-bound beta-subunit | Vibrio cholerae serotype O1 |
Synonyms | Comment | Organism |
---|---|---|
OADC | - |
Klebsiella aerogenes |
OADC | - |
Vibrio cholerae serotype O1 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
biotin | dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate | Klebsiella aerogenes | |
biotin | dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate | Vibrio cholerae serotype O1 |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the class II decarboxylases of the biotin-dependent enzyme family. Class II enzymes facilitate sodium transport from the cytoplasm to the periplasm in some archaea and anaerobic bacteria | Klebsiella aerogenes |
evolution | the enzyme belongs to the class II decarboxylases of the biotin-dependent enzyme family. Class II enzymes facilitate sodium transport from the cytoplasm to the periplasm in some archaea and anaerobic bacteria | Vibrio cholerae serotype O1 |
additional information | oxaloacetate decarboxylase complex structure, modeling, overview. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place. The gamma-subunit significantly accelerates the rate of oxaloacetate decarboxylation in the alpha-subunit, which correlates with the coordination of a Zn2+ metal ion by several residues at the hydrophilic C-terminus. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place | Klebsiella aerogenes |
additional information | oxaloacetate decarboxylase complex structure, modeling, overview. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place. The gamma-subunit significantly accelerates the rate of oxaloacetate decarboxylation in the alpha-subunit, which correlates with the coordination of a Zn2+ metal ion by several residues at the hydrophilic C-terminus. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place | Vibrio cholerae serotype O1 |
physiological function | the membrane-bound oxaloacetate decarboxylase complex of Klebsiella aerogenes catalyzes the biotin-dependent decarboxylation of oxaloacetate, while also serves as a primary Na+ pump. The enzyme complex plays an essential role in the citrate or tartrate fermentation pathways of certain archaea and bacteria, contributing to the generation of an electrochemical gradient of Na+ ions along with one mol of ATP per mol of citrate/tartrate. The resulting Na+ gradient is used to power the import of nutrients and the synthesis of ATP | Klebsiella aerogenes |