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UniProt functional annotation for P9WNG3 | ||
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| UniProt code: P9WNG3. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| Function: | |
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Possesses a clear preference for long- chain acyl-CoA substrates rather than acyl-ACP primers, and shows only weak activity with acetyl-CoA. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}. |
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| Catalytic activity: | |
Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815}; |
| Catalytic activity: | |
Reaction=H(+) + hexanoyl-CoA + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42256, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9633, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:78449, ChEBI:CHEBI:78460; Evidence={ECO:0000269|PubMed:11278743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42257; Evidence={ECO:0000269|PubMed:11278743}; |
| Catalytic activity: | |
Reaction=H(+) + malonyl-[ACP] + octanoyl-CoA = 3-oxodecanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42264, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9637, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:78449, ChEBI:CHEBI:78464; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42265; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; |
| Catalytic activity: | |
Reaction=decanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:43652, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:78449, ChEBI:CHEBI:78469; Evidence={ECO:0000269|PubMed:10840036}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43653; Evidence={ECO:0000269|PubMed:10840036}; |
| Catalytic activity: | |
Reaction=dodecanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl- [ACP] + CO2 + CoA; Xref=Rhea:RHEA:43640, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9645, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43641; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; |
| Catalytic activity: | |
Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-CoA = 3-oxohexadecanoyl- [ACP] + CO2 + CoA; Xref=Rhea:RHEA:43644, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9649, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:78449, ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43645; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; |
| Catalytic activity: | |
Reaction=H(+) + hexadecanoyl-CoA + malonyl-[ACP] = 3-oxooctadecanoyl- [ACP] + CO2 + CoA; Xref=Rhea:RHEA:43648, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9653, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:78449, ChEBI:CHEBI:78487; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43649; Evidence={ECO:0000269|PubMed:10840036, ECO:0000269|PubMed:11278743}; |
| Activity regulation: | |
Sensitive to thiolactomycin and resistant to cerulenin in vitro. {ECO:0000269|PubMed:10840036}. |
| Pathway: | |
Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP- Rule:MF_01815}. |
| Pathway: | |
Lipid metabolism; mycolic acid biosynthesis. {ECO:0000305|PubMed:10840036}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:11278743}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}. |
| Domain: | |
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH. {ECO:0000255|HAMAP- Rule:MF_01815}. |
| Miscellaneous: | |
Was identified as a high-confidence drug target. {ECO:0000269|PubMed:19099550}. |
| Similarity: | |
Belongs to the thiolase-like superfamily. FabH family. {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.