MccA is the biotin-carboxylase and biotin-carrier alpha subunit of bacterial 3-methylcrotonyl-CoA carboxylase. In the assembled MCC complex it uses ATP and bicarbonate to carboxylate its covalently attached biotin, enabling MccB to carboxylate 3-methylcrotonyl-CoA during distal L-leucine catabolism.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: Nucleotide binding is implicit in ATP-dependent biotin carboxylation. Reason: Retain this valid but broad binding activity as non-core beside the enzyme-specific biotin carboxylase activity. |
| GO:0004075 biotin carboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct alpha-subunit catalytic activity. Reason: MccA contains the biotin-carboxylase and biotin-carrier domains. Supporting Evidence: file:PSEPK/mccA/mccA-uniprot.txt InterPro; IPR011764; Biotin_carboxylation_dom. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: ATP binding is mechanistically correct but redundant. Reason: ATP binding is a genuine co-annotatable function of the ATP-grasp biotin-carboxylase domain, but is not the core reaction. |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Generic metal binding does not identify the MCC reaction role. Reason: Retain the mechanistically compatible cofactor-binding annotation as non-core; the specific catalytic activity provides the useful reaction annotation. |
| GO:0009374 biotin binding | ISM file:PSEPK/mccA/mccA-uniprot.txt | NEW | Summary: MccA contains the biotin-carrier domain and the conserved biotin attachment motif. Reason: Covalently attached biotin is the mobile carboxyl carrier between the alpha-subunit biotin-carboxylase site and the beta-subunit carboxyltransferase site. Supporting Evidence: file:PSEPK/mccA/mccA-uniprot.txt InterPro; IPR000089; Biotin_lipoyl. file:PSEPK/mccA/mccA-uniprot.txt PROSITE; PS00188; BIOTIN; 1. |
| GO:0004485 methylcrotonoyl-CoA carboxylase activity | ISS PMID:16272386 Methylcrotonyl-CoA and geranyl-CoA carboxylases are involved... | NEW | Summary: MccA supplies biotin carboxylase and carrier functions to the two-subunit MCC holoenzyme. Reason: The complete substrate-specific reaction is a property of assembled MccA-MccB, so contributes_to is more precise than enables for the alpha subunit. Supporting Evidence: PMID:16272386 The two subunits of MCase corresponded to liuB/liuD file:PSEPK/mccA/mccA-uniprot.txt InterPro; IPR048429; MCC_alpha_BT. |
| GO:0006552 L-leucine catabolic process | ISS PMID:16272386 Methylcrotonyl-CoA and geranyl-CoA carboxylases are involved... | NEW | Summary: The MCC-alpha domain assignment and conserved ivd-mccB-liuC-mccA cluster support a role in distal L-leucine catabolism. Reason: This informative pathway term is absent from the current GOA set. Supporting Evidence: PMID:16272386 The two subunits of MCase corresponded to liuB/liuD file:PSEPK/mccA/mccA-uniprot.txt InterPro; IPR048429; MCC_alpha_BT. |
| GO:1905202 methylcrotonoyl-CoA carboxylase complex | ISS PMID:16272386 Methylcrotonyl-CoA and geranyl-CoA carboxylases are involved... | NEW | Summary: MccA is the biotin-carboxylase/carrier alpha subunit of bacterial MCC. Reason: Complex membership captures the cooperative MccA-MccB reaction architecture. Supporting Evidence: PMID:16272386 The two subunits of MCase corresponded to liuB/liuD file:PSEPK/mccA/mccA-uniprot.txt InterPro; IPR048429; MCC_alpha_BT. |
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Download this section (compressed HTML)Experiment: Reconstitute MccA with MccB and quantify ATP-dependent 3-methylcrotonyl-CoA carboxylation; compare against MccA alone.
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