4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase

Details

Name
4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase
Synonyms
  • 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase
  • 3.7.1.17
  • bphD
  • HOPDA hydrolase
  • MCP hydrolase
  • Meta-cleavage product hydrolase
Gene Name
hsaD
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051255|4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase
MTATEELTFESTSRFAEVDVDGPLKLHYHEAGVGNDQTVVLLHGGGPGAASWTNFSRNIA
VLARHFHVLAVDQPGYGHSDKRAEHGQFNRYAAMALKGLFDQLGLGRVPLVGNSLGGGTA
VRFALDYPARAGRLVLMGPGGLSINLFAPDPTEGVKRLSKFSVAPTRENLEAFLRVMVYD
KNLITPELVDQRFALASTPESLTATRAMGKSFAGADFEAGMMWREVYRLRQPVLLIWGRE
DRVNPLDGALVALKTIPRAQLHVFGQCGHWVQVEKFDEFNKLTIEFLGGGR
Number of residues
291
Molecular Weight
31875.21
Theoretical pI
Not Available
GO Classification
Functions
2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity / 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase activity / 4,9-DSHA hydrolase activity
Processes
aromatic compound catabolic process / growth of symbiont in host / lipid catabolic process / steroid biosynthetic process
Components
cell wall / plasma membrane
General Function
Catalyzes the hydrolysis of a carbon-carbon bond in 4,5: 9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate (4,9-DSHA) to yield 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oate (DOHNAA) and 2-hydroxy-hexa-2,4-dienoate (HHD). Is also able to catalyze the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) and the synthetic analog 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid (HOPODA).
Specific Function
2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051256|4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase (hsaD)
ATGACAGCTACCGAGGAATTGACGTTCGAATCCACCTCGCGCTTTGCGGAAGTGGACGTC
GACGGGCCGCTGAAACTGCACTACCACGAGGCCGGCGTGGGCAACGACCAGACGGTGGTG
CTACTGCACGGCGGTGGGCCCGGCGCGGCGAGCTGGACGAACTTCTCGCGTAATATCGCG
GTGCTGGCGCGGCACTTTCATGTGCTGGCCGTCGACCAGCCCGGTTACGGCCATTCCGAC
AAGCGGGCCGAGCACGGCCAGTTCAATCGCTATGCCGCGATGGCGCTGAAGGGGCTCTTC
GATCAGCTGGGGCTGGGGCGGGTACCGCTGGTGGGCAACTCGTTGGGCGGGGGAACCGCG
GTCCGGTTTGCGCTGGACTACCCGGCCCGGGCAGGACGGTTAGTGCTGATGGGCCCGGGG
GGCCTGAGTATCAACCTGTTTGCGCCCGACCCGACCGAGGGAGTCAAACGGCTGTCGAAG
TTCTCCGTTGCGCCCACCCGGGAGAACCTCGAGGCGTTCCTGCGGGTCATGGTCTACGAC
AAGAACCTGATCACCCCCGAGTTGGTGGATCAGCGGTTTGCGCTGGCCAGCACCCCGGAG
TCGTTGACGGCAACACGGGCGATGGGAAAGTCGTTCGCCGGAGCCGACTTCGAGGCCGGC
ATGATGTGGCGCGAGGTGTATCGGCTGCGCCAGCCGGTGTTGCTGATCTGGGGTCGTGAG
GACCGGGTCAACCCGCTGGACGGCGCGCTGGTTGCGTTGAAAACGATTCCGCGTGCGCAG
CTGCACGTATTCGGGCAGTGTGGGCATTGGGTGCAGGTGGAGAAGTTCGACGAGTTCAAC
AAGCTGACGATTGAATTTCTGGGAGGTGGCAGATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WNH5
UniProtKB Entry NameHSAD_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Kendall SL, Withers M, Soffair CN, Moreland NJ, Gurcha S, Sidders B, Frita R, Ten Bokum A, Besra GS, Lott JS, Stoker NG: 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. [Article]
  3. Van der Geize R, Yam K, Heuser T, Wilbrink MH, Hara H, Anderton MC, Sim E, Dijkhuizen L, Davies JE, Mohn WW, Eltis LD: A gene cluster encoding cholesterol catabolism in a soil actinomycete provides insight into Mycobacterium tuberculosis survival in macrophages. Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1947-52. Epub 2007 Jan 30. [Article]
  4. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: 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. [Article]
  5. Lack N, Lowe ED, Liu J, Eltis LD, Noble ME, Sim E, Westwood IM: Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):2-7. Epub 2007 Dec 20. [Article]
  6. Lack NA, Yam KC, Lowe ED, Horsman GP, Owen RL, Sim E, Eltis LD: Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism. J Biol Chem. 2010 Jan 1;285(1):434-43. doi: 10.1074/jbc.M109.058081. Epub 2009 Oct 29. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07911(3E)-2,6-DIOXO-6-PHENYLHEX-3-ENOATEexperimentalunknownDetails