fadD19
- Type
- protein_coding
- Name
- fadD19
- Locus Name
-
Rv3515c
- Product
-
Fatty-acid-CoA ligase FadD19 (fatty-acid-CoA synthetase) (fatty-acid-CoA synthase)
- Functional Category
-
Lipid metabolism
- Location
- 3950824..3952470 (- strand)
- Gene Length
- 1646 bp
- Nucleotides
-
GTGGCCGTGGCCCTGAATATTGCCGATCTCGCCGAGCACGCCATCGACGCCGTGCCTGACCGTGTCGCCGTTATCTGCGGCGATGAGCAGTTGACCTACGCCCAGCTGGAGGATAAGGCCAACCGCCTCGCGCACCACCTGATCGATCAAGGCGTGCAAAAGGACGACAAGGTCGGCCTGTACTGCCGCAACCGCATCGAGATCGTGATCGCGATGCTGGGCATCGTGAAGGCGGGCGCCATCTTGGTGAACGTCAACTTCCGTTACGTGGAGGGCGAACTTCGCTACCTGTTCGACAACTCCGACATGGTCGCGTTGGTGCACGAACGCCGCTACGCCGACCGGGTCGCCAACGTTCTCCCCGACACGCCCCATGTAAGGACGATCTTGGTCGTCGAGGACGGCTCGGACCAGGACTATCGGCGCTACGGCGGCGTCGAGTTCTATTCCGCGATCGCGGCGGGCTCGCCGGAGCGTGACTTCGGCGAACGCAGCGCCGACGCCATCTATCTGCTCTACACCGGCGGCACCACCGGTTTCCCCAAGGGTGTGATGTGGCGTCACGAGGACATCTATCGTGTGCTGTTCGGTGGAACCGACTTTGCGACAGGAGAGTTCGTCAAAGACGAATACGACCTGGCCAAGGCGGCCGCGGCGAATCCACCGATGATCCGCTACCCGATCCCGCCGATGATCCACGGCGCCACCCAGTCGGCCACCTGGATGGCGCTCTTCTCGGGCCAAACCACGGTACTGGCACCGGAATTCAACGCCGACGAGGTGTGGCGCACGATCCACAAACACAAGGTGAACCTGCTGTTCTTCACCGGTGATGCGATGGCCCGCCCGCTGGTCGACGCGCTGGTCAAGGGCAACGACTACGACCTGTCGTCGTTGTTCCTGTTGGCCAGCACCGCGGCGCTGTTCTCGCCGAGCATCAAGGAGAAACTCCTTGAGCTGCTGCCGAATCGGGTGATCACGGACTCAATTGGCTCGTCGGAGACGGGTTTTGGCGGTACCAGCGTCGTTGCTGCCGGGCAGGCGCATGGCGGCGGGCCCCGGGTGCGGATCGACCATCGCACCGTCGTGCTCGATGACGACGGCAACGAAGTCAAGCCCGGCTCGGGGATGCGGGGCGTCATCGCCAAGAAGGGCAACATTCCCGTCGGCTACTACAAGGACGAGAAGAAGACGGCCGAGACGTTCCGGACGATTAACGGTGTGCGCTACGCCATTCCGGGGGACTACGCCCAAGTCGAGGAGGACGGCACGGTCACCATGCTGGGTCGTGGCTCGGTGTCGATCAACAGCGGCGGCGAGAAGGTCTACCCCGAAGAGGTCGAGGCCGCTTTGAAGGGGCATCCCGACGTGTTCGACGCTCTGGTGGTCGGGGTGCCCGATCCGCGTTACGGCCAGCAGGTGGCCGCCGTGGTGCAGGCCCGGCCGGGTTGTCGGCCGTCGTTGGCCGAGTTGGACTCGTTCGTGCGCTCCGAGATCGCGGGCTACAAAGTGCCGCGCAGTCTGTGGTTTGTCGACGAGGTGAAGCGTTCGCCCGCCGGTAAGCCGGACTACCGCTGGGCCAAGGAGCAGACCGAGGCGCGGCCAGCCGATGACGTGCATGCGGGACACGTGACGAGCGGTGGGTG
- Drug Resistance
- Mutations
- Function
- Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Also involved in the degradation of cholesterol via the degradation of the side chains of C-24 branched-chain sterols. Catalyzes the ATP-dependent CoA thioesterification of the sterol 3-oxocholest-4-en-26-oate to yield 3-oxocholest-4-en-26-oyl-CoA. It can also use 3beta-hydroxy-5-cholesten-26-oate. {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:24244004}.
- Family
-
ATP-dependent AMP-binding enzyme family
- GO
-
- fatty acid biosynthetic process GO:0006633 biological_process
- decanoate-CoA ligase activity GO:0102391 molecular_function
- long-chain fatty acid-CoA ligase activity GO:0004467 molecular_function
- cholesterol metabolic process GO:0008203 biological_process
- response to host immune response GO:0052572 biological_process
- ATP binding GO:0005524 molecular_function
- cell wall GO:0005618 cellular_component
- lipid biosynthetic process GO:0008610 biological_process
- acyl-CoA ligase activity GO:0003996 molecular_function
- Actinobacterium-type cell wall biogenesis GO:0071766 biological_process
- InterPro
Summary
- Name
- Long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase (FACL) (EC 6.2.1.3) (EC 6.2.1.42) (Acyl-CoA synthetase) (Steroid-CoA ligase) (Steroid-coenzyme A ligase)
- Family
- ATP-dependent AMP-binding enzyme family
- Protein Sequence
-
MAVALNIADLAEHAIDAVPDRVAVICGDEQLTYAQLEDKANRLAHHLIDQGVQKDDKVGLYCRNRIEIVIAMLGIVKAGAILVNVNFRYVEGELRYLFDNSDMVALVHERRYADRVANVLPDTPHVRTILVVEDGSDQDYRRYGGVEFYSAIAAGSPERDFGERSADAIYLLYTGGTTGFPKGVMWRHEDIYRVLFGGTDFATGEFVKDEYDLAKAAAANPPMIRYPIPPMIHGATQSATWMALFSGQTTVLAPEFNADEVWRTIHKHKVNLLFFTGDAMARPLVDALVKGNDYDLSSLFLLASTAALFSPSIKEKLLELLPNRVITDSIGSSETGFGGTSVVAAGQAHGGGPRVRIDHRTVVLDDDGNEVKPGSGMRGVIAKKGNIPVGYYKDEKKTAETFRTINGVRYAIPGDYAQVEEDGTVTMLGRGSVSINSGGEKVYPEEVEAALKGHPDVFDALVVGVPDPRYGQQVAAVVQARPGCRPSLAELDSFVRSEIAGYKVPRSLWFVDEVKRSPAGKPDYRWAKEQTEARPADDVHAGHVTSGG
- Mass
- 59,741 Da
- Length
- 548 Aa
Rv3515c doesn't seem to be a targeted by any drug.
Rv3515c doesn't seem to be involved in any pathway.
- Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain catabolism.
- J Bacteriol. 2014 Feb;196(3):579-87. doi: 10.1128/JB.01012-13. Epub 2013 Nov 15.
- Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
- Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
- Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria.
- Nature. 2004 Mar 25;428(6981):441-5. doi: 10.1038/nature02384.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.