kshA
- Type
- protein_coding
- Name
- kshA
- Locus Name
-
Rv3526
- Product
-
Oxygenase component of 3-ketosteroid-9-alpha-hydroxylase KshA
- Functional Category
-
Intermediary metabolism and respiration
- Location
- 3962439..3963599 (+ strand)
- Gene Length
- 1160 bp
- Nucleotides
-
TGAGTACCGACACGAGTGGGGTCGGTGTTCGGGAGATCGATGCCGGCGCCTTGCCGACCAGGTATGCGCGTGGCTGGCATTGCCTGGGCGTCGCGAAGGACTATTTGGAAGGGAAGCCACACGGGGTAGAGGCGTTCGGCACCAAGCTGGTTGTGTTCGCTGATTCCCACGGGGACCTGAAAGTCCTCGACGGCTACTGCCGGCACATGGGCGGCGACCTGTCCGAGGGCACCGTCAAAGGCGACGAGGTCGCTTGCCCGTTCCACGACTGGCGCTGGGGTGGCGACGGCCGCTGCAAATTGGTGCCGTATGCCAGGCGCACACCCAGAATGGCGCGCACTCGGTCGTGGACGACCGATGTGCGCAGCGGGCTGCTGTTTGTCTGGCACGACCATGAGGGCAATCCACCCGACCCCGCGGTCCGGATCCCCGAGATTCCCGAGGCGGCCAGCGACGAGTGGACCGACTGGCGGTGGAACCGCATCCTCATCGAAGGGTCCAACTGCCGCGACATCATCGACAACGTCACCGATATGGCGCACTTCTTCTACATCCACTTCGGTTTGCCGACGTACTTCAAGAACGTCTTCGAGGGCCACATCGCCTCGCAGTATCTGCACAACGTGGGCCGGCCCGATGTCGACGATCTGGGGACGTCTTACGGTGAGGCGCATCTGGATTCGGAGGCGTCTTACTTCGGGCCGTCGTTCATGATCAACTGGCTGCACAACCGCTACGGCAACTACAAGTCCGAGTCGATCCTGATCAACTGCCACTACCCGGTGACCCAGAACTCGTTCGTCCTGCAATGGGGCGTCATCGTCGAAAAGCCCAAGGGTATGAGCGAAGAGATGACCGACAAGTTGTCGCGGGTGTTCACCGAGGGCGTCAGCAAGGGCTTCTTGCAGGATGTCGAGATCTGGAAGCACAAGACCCGCATCGACAACCCGCTGCTGGTTGAAGAGGACGGCGCCGTGTATCAGCTGCGCCGCTGGTATGAACAGTTTTATGTCGACGTAGCCGACATAAAACCAGAGATGGTGGAGCGCTTCGAGATCGAGGTCGACACCAAGCGCGCCAACGAGTTCTGGAATGCCGAGGTAGAGAAGAACTTGAAATCGAGAGAAGTTTCCGACGACGTGCCCGCCGAGCAACACTGA
- Drug Resistance
- Mutations
- Function
- Involved in the degradation of cholesterol. Catalyzes the introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) intermediate which spontaneously form 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (HSA) via the meta-cleavage of ring B with concomitant aromatization of ring A. KSH is also able to use 4-androstene-3,17-dione (AD), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC), 3-oxo-23,24-bisnorcholesta-4-en-22-oyl-coenzyme A thioester (4-BNC-CoA) and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) as substrates. {ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:21987574}.
- Family
-
Unknown
- GO
-
- steroid biosynthetic process GO:0006694 biological_process
- cholesterol catabolic process GO:0006707 biological_process
- protein homotrimerization GO:0070207 biological_process
- response to cholesterol GO:0070723 biological_process
- 2 iron, 2 sulfur cluster binding GO:0051537 molecular_function
- ketosteroid monooxygenase activity GO:0047086 molecular_function
- iron ion binding GO:0005506 molecular_function
- pathogenesis GO:0009405 biological_process
- 3-ketosteroid 9-alpha-monooxygenase activity GO:0036200 molecular_function
- InterPro
2ZYL
- Name
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (3-ketosteroid-9-alpha-hydroxylase, oxygenase component) (KSH) (Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase) (EC 1.14.15.30) (Rieske-type oxygenase) (RO)
- Family
- Unknown
- Protein Sequence
-
MSTDTSGVGVREIDAGALPTRYARGWHCLGVAKDYLEGKPHGVEAFGTKLVVFADSHGDLKVLDGYCRHMGGDLSEGTVKGDEVACPFHDWRWGGDGRCKLVPYARRTPRMARTRSWTTDVRSGLLFVWHDHEGNPPDPAVRIPEIPEAASDEWTDWRWNRILIEGSNCRDIIDNVTDMAHFFYIHFGLPTYFKNVFEGHIASQYLHNVGRPDVDDLGTSYGEAHLDSEASYFGPSFMINWLHNRYGNYKSESILINCHYPVTQNSFVLQWGVIVEKPKGMSEEMTDKLSRVFTEGVSKGFLQDVEIWKHKTRIDNPLLVEEDGAVYQLRRWYEQFYVDVADIKPEMVERFEIEVDTKRANEFWNAEVEKNLKSREVSDDVPAEQH
- Mass
- 44,268 Da
- Length
- 386 Aa
Summary
Rv3526 doesn't seem to be a targeted by any drug.
-
-
Steroid degradation mtu00984
mtu00984PATHWAY_MAP mtu00984 Steroid degradation
-
- Substrate specificities and conformational flexibility of 3-ketosteroid 9alpha-hydroxylases.
- J Biol Chem. 2014 Sep 12;289(37):25523-36. doi: 10.1074/jbc.M114.575886. Epub 2014 Jul 21.
- Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis.
- J Biol Chem. 2009 Apr 10;284(15):9937-46. doi: 10.1074/jbc.M900719200. Epub 2009 Feb 20.
- 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.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.
- A highly conserved transcriptional repressor controls a large regulon involved in lipid degradation in Mycobacterium smegmatis and Mycobacterium tuberculosis.
- Mol Microbiol. 2007 Aug;65(3):684-99. doi: 10.1111/j.1365-2958.2007.05827.x.
- Activity of 3-ketosteroid 9alpha-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis.
- J Biol Chem. 2011 Nov 25;286(47):40717-24. doi: 10.1074/jbc.M111.289975. Epub 2011 Oct 10.