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Literature summary extracted from

  • Lietzan, A.D.; St Maurice, M.
    Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity (2014), Arch. Biochem. Biophys., 544, 75-86.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.112 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
-
4.1.1.112 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

EC Number Metals/Ions Comment Organism Structure
4.1.1.112 Zn2+ bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus Klebsiella aerogenes
4.1.1.112 Zn2+ bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.112 additional information Klebsiella aerogenes decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview ?
-
 ?
4.1.1.112 additional information Vibrio cholerae serotype O1 decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview ?
-
 ?
4.1.1.112 Oxaloacetate Klebsiella aerogenes
-
 Pyruvate + CO2
-
 ?
4.1.1.112 Oxaloacetate Vibrio cholerae serotype O1
-
 Pyruvate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.112 Klebsiella aerogenes
-
-
-
4.1.1.112 Vibrio cholerae serotype O1
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.112 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
a
4.1.1.112 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.112 additional information decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview Klebsiella aerogenes ?
-
 ?
4.1.1.112 additional information decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview Vibrio cholerae serotype O1 ?
-
 ?
4.1.1.112 Oxaloacetate
-
 Klebsiella aerogenes Pyruvate + CO2
-
 ?
4.1.1.112 Oxaloacetate
-
 Vibrio cholerae serotype O1 Pyruvate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.112 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
4.1.1.112 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
4.1.1.112 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

EC Number Synonyms Comment Organism
4.1.1.112 OADC
-
 Klebsiella aerogenes
4.1.1.112 OADC
-
 Vibrio cholerae serotype O1

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.112 biotin dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate Klebsiella aerogenes
4.1.1.112 biotin dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate Vibrio cholerae serotype O1

General Information

EC Number General Information Comment Organism
4.1.1.112 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
4.1.1.112 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
4.1.1.112 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
4.1.1.112 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
4.1.1.112 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