| IED ID | IndEnz0002002988 |
| Enzyme Type ID | protease002988 |
| Protein Name |
3-oxoacyl- acyl-carrier-protein synthase 1 EC 2.3.1.293 Beta-ketoacyl-ACP synthase 1 KAS 1 |
| Gene Name | kasA ERDMAN_2470 |
| Organism | Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
| Enzyme Sequence | MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY |
| Enzyme Length | 416 |
| Uniprot Accession Number | H8ESN0 |
| Absorption | |
| Active Site | ACT_SITE 171; /evidence=ECO:0000250|UniProtKB:P9WQD9 |
| Activity Regulation | |
| Binding Site | BINDING 311; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P9WQD9; BINDING 345; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P9WQD9 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an ultra-long-chain mono-unsaturated fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxo-ultra-long-chain mono-unsaturated fatty acyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:65312, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16765, Rhea:RHEA-COMP:16775, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:156399, ChEBI:CHEBI:156400; EC=2.3.1.293; Evidence={ECO:0000250|UniProtKB:P9WQD9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65313; Evidence={ECO:0000250|UniProtKB:P9WQD9}; |
| DNA Binding | |
| EC Number | 2.3.1.293 |
| Enzyme Function | FUNCTION: Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the elongation of long chain acyl-ACP substrates by the addition of two carbons from malonyl-ACP to an acyl acceptor. Involved in the initial extension of the mycolate chain and forms monounsaturated fatty acids that averaged 40 carbons in length. {ECO:0000250|UniProtKB:P9WQD9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000250|UniProtKB:P9WQD9}. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1) |
| Keywords | Acyltransferase;Cytoplasm;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Transferase |
| Interact With | |
| Induction | INDUCTION: Repressed by Rip1 and independently by the metal chelator phenanthroline. {ECO:0000269|PubMed:20545848}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WQD9}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,316 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:65312; RHEA:65313 |
| Cross Reference Brenda |