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Showing Protein 3-oxosteroid 1-dehydrogenase (HMDBP12592)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP12592
Secondary Accession Numbers None
Name 3-oxosteroid 1-dehydrogenase
Synonyms
  1. 3-keto-Delta(4)-steroid Delta(1)-dehydrogenase
  2. 3-oxo-Delta(4)-steroid 1-dehydrogenase
  3. KSDD
  4. KSTD
Gene Name KSTD
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Involved in the degradation of cholesterol (PubMed:18031290, PubMed:21987574). Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids (PubMed:18031290). Has a clear preference for 3-ketosteroids with a saturated A-ring, displaying highest activity on 5alpha-AD (5alpha-androstane-3,17-dione) and 5alpha-T (5alpha-testosterone, also known as 17beta-hydroxy-5alpha-androstane-3-one) (PubMed:18031290). Is also involved in the formation of 3-keto-1,4-diene-steroid from 3-keto-4-ene-steroid (PubMed:21987574). Catalyzes the conversion of 3-oxo-23,24-bisnorchol-4-en-22-oyl-coenzyme A thioester (4-BNC-CoA) to 3-oxo-23,24-bisnorchola-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) (PubMed:21987574).
Pathways
  • Microbial metabolism in diverse environments
  • Steroid degradation
Reactions Not Available
GO Classification
Biological Process
steroid biosynthetic process
cholesterol catabolic process
pathogenesis
Cellular Component
plasma membrane
Molecular Function
3-oxosteroid 1-dehydrogenase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 563
Molecular Weight 60635.61
Theoretical pI 8.198
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P71864
UniProtKB/Swiss-Prot Entry Name 3O1D_MYCTU
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
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. doi: 10.1038/31159. [PubMed:9634230 ]
  2. 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. [PubMed:21969609 ]
  3. Knol J, Bodewits K, Hessels GI, Dijkhuizen L, van der Geize R: 3-Keto-5alpha-steroid Delta(1)-dehydrogenase from Rhodococcus erythropolis SQ1 and its orthologue in Mycobacterium tuberculosis H37Rv are highly specific enzymes that function in cholesterol catabolism. Biochem J. 2008 Mar 1;410(2):339-46. doi: 10.1042/BJ20071130. [PubMed:18031290 ]
  4. Capyk JK, Casabon I, Gruninger R, Strynadka NC, Eltis LD: 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. [PubMed:21987574 ]
  5. Brzezinska M, Szulc I, Brzostek A, Klink M, Kielbik M, Sulowska Z, Pawelczyk J, Dziadek J: The role of 3-ketosteroid 1(2)-dehydrogenase in the pathogenicity of Mycobacterium tuberculosis. BMC Microbiol. 2013 Feb 20;13:43. doi: 10.1186/1471-2180-13-43. [PubMed:23425360 ]