Rv3406
- Type
- protein_coding
- Name
- Rv3406
- Locus Name
-
Rv3406
- Product
-
Probable dioxygenase
- Functional Category
-
Intermediary metabolism and respiration
- Location
- 3825330..3826217 (+ strand)
- Gene Length
- 887 bp
- Nucleotides
-
TGACAGATCTGATTACCGTGAAGAAGCTGGGCAGCCGTATCGGCGCCCAAATCGACGGGGTGCGCCTCGGAGGCGATCTGGACCCCGCCGCAGTCAACGAGATTCGCGCGGCACTACTGGCCCACAAGGTGGTCTTCTTCCGCGGTCAGCACCAACTCGATGACGCCGAGCAGCTGGCGTTTGCCGGGTTACTGGGCACCCCGATCGGCCACCCGGCCGCGATCGCCCTCGCCGACGATGCACCGATCATCACGCCGATCAACTCCGAGTTCGGCAAGGCGAACCGCTGGCACACCGACGTCACGTTCGCCGCCAACTATCCGGCCGCCTCGGTACTGCGCGCGGTCTCCCTGCCCAGCTATGGCGGGTCGACGTTGTGGGCCAACACCGCCGCGGCCTACGCGGAGCTGCCCGAGCCGCTCAAGTGCCTCACCGAAAACCTGTGGGCGCTGCACACCAACCGCTATGACTACGTCACGACCAAACCGCTGACCGCGGCGCAGCGGGCCTTCCGTCAGGTGTTCGAGAAGCCGGACTTCCGCACCGAGCATCCCGTGGTGCGGGTACACCCGGAGACCGGTGAGCGCACGCTGCTAGCGGGCGACTTCGTGCGCAGCTTCGTCGGGTTGGACAGCCACGAATCAAGGGTGTTATTCGAAGTGCTGCAACGGCGAATCACCATGCCCGAAAACACCATCCGCTGGAACTGGGCGCCGGGCGACGTAGCCATCTGGGACAACCGGGCCACCCAACACCGGGCGATCGACGACTACGACGACCAGCACCGGCTGATGCACCGGGTCACCTTGATGGGCGACGTGCCCGTCGACGTGTACGGGCAGGCTAGCCGGGTGATCAGCGGGGCGCCGATGGAGATCGCTGGCTGA
- Drug Resistance
- Mutations
- Function
- Alpha-ketoglutarate-dependent sulfate ester dioxygenase, which oxidizes medium-chain alkyl-sulfate esters (PubMed:23762287). Shows preference for 2-ethylhexyl sulfate (2-EHS) in vitro, leading to the formation of succinate and 2-ethylhexanal (PubMed:23762287, PubMed:25427196). Has likely a role in sulfate scavenging in vivo (PubMed:23762287). {ECO:0000269|PubMed:23762287, ECO:0000269|PubMed:25427196}.; FUNCTION: Also causes the inactivation of the 2-carboxyquinoxaline Ty38c (an antitubercular compound that inhibits DprE1) via oxidative decarboxylation, using Ty38c instead of alpha-ketoglutarate as a substrate. Is thus responsible for primary resistance of M.tuberculosis to Ty38c in vitro. Overexpression of Rv3406 causes resistance to Ty38c. {ECO:0000269|PubMed:25427196}.
- Family
-
TfdA dioxygenase family
- GO
-
- sulfur compound catabolic process GO:0044273 biological_process
- metal ion binding GO:0046872 molecular_function
- response to antibiotic GO:0046677 biological_process
- sulfonate dioxygenase activity GO:0000907 molecular_function
- taurine dioxygenase activity GO:0000908 molecular_function
- plasma membrane GO:0005886 cellular_component
- cytoplasm GO:0005737 cellular_component
- InterPro
4CVY
- Name
- Alpha-ketoglutarate-dependent sulfate ester dioxygenase (EC 1.14.11.-) (Type II alkyl sulfatase)
- Family
- TfdA dioxygenase family
- Protein Sequence
-
MTDLITVKKLGSRIGAQIDGVRLGGDLDPAAVNEIRAALLAHKVVFFRGQHQLDDAEQLAFAGLLGTPIGHPAAIALADDAPIITPINSEFGKANRWHTDVTFAANYPAASVLRAVSLPSYGGSTLWANTAAAYAELPEPLKCLTENLWALHTNRYDYVTTKPLTAAQRAFRQVFEKPDFRTEHPVVRVHPETGERTLLAGDFVRSFVGLDSHESRVLFEVLQRRITMPENTIRWNWAPGDVAIWDNRATQHRAIDDYDDQHRLMHRVTLMGDVPVDVYGQASRVISGAPMEIAG
- Mass
- 32,579 Da
- Length
- 295 Aa
Summary
Rv3406 doesn't seem to be a targeted by any drug.
Rv3406 doesn't seem to be involved in any pathway.
- 2-Carboxyquinoxalines kill mycobacterium tuberculosis through noncovalent inhibition of DprE1.
- ACS Chem Biol. 2015 Mar 20;10(3):705-14. doi: 10.1021/cb5007163. Epub 2014 Dec 9.
- Mycobacterium tuberculosis Rv3406 is a type II alkyl sulfatase capable of sulfate scavenging.
- PLoS One. 2013 Jun 6;8(6):e65080. doi: 10.1371/journal.pone.0065080. Print 2013.
- Biophysical and biochemical characterization of Rv3405c, a tetracycline repressor protein from Mycobacterium tuberculosis.
- Biochem Biophys Res Commun. 2018 Feb 12;496(3):799-805. doi: 10.1016/j.bbrc.2018.01.152.
- 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.
- targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis.
- BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.