KEGG   ENZYME: 1.14.13.142Help
Entry
EC 1.14.13.142              Enzyme                                 

Name
3-ketosteroid 9alpha-monooxygenase;
KshAB;
3-ketosteroid 9alpha-hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
androsta-1,4-diene-3,17-dione,NADH:oxygen oxidoreductase (9alpha-hydroxylating)
Reaction(IUBMB)
androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O [RN:R09860]
Reaction(KEGG)
Substrate
androsta-1,4-diene-3,17-dione [CPD:C20144];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
9alpha-hydroxyandrosta-1,4-diene-3,17-dione [CPD:C14909];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Comment
The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It is a two-component system consisting of a terminal oxygenase (KshA) and a ferredoxin reductase (KshB). The oxygenase contains a Rieske-type iron-sulfur center and non-heme iron. The reductase component is a flavoprotein containing an NAD-binding domain and a plant-type iron-sulfur cluster. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
History
EC 1.14.13.142 created 2012
Pathway
ec00984  Steroid degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K15982  3-ketosteroid 9alpha-monooxygenase subunit A
K15983  3-ketosteroid 9alpha-monooxygenase subunit B
Genes
PSG: G655_23840
PRE: PCA10_12240(kshA) PCA10_43650(kshB)
PPUT: L483_14105 L483_14320
PPUN: PP4_26740(kshA) PP4_27180(kshB)
PVR: PverR02_11715 PverR02_11735
PSC: A458_17160
PSH: Psest_3453
PSTU: UIB01_04060
PBM: CL52_03850 CL52_10355
PPUU: PputUW4_01666 PputUW4_01678
PKC: PKB_4313(ksha1) PKB_4319(kshB) PKB_4338(ksha3)
PTN: PTRA_a1005(kshB) PTRA_a2590(kshA)
PNG: PNIG_a1057(kshB) PNIG_a2784(kshA)
REH: H16_B0643(h16_B0643) H16_B0672(hcaE)
BCEN: DM39_3466 DM39_6206(hmp) DM39_6233(kshA)
BCED: DM42_6314(hmp) DM42_6338(kshA)
NAR: Saro_3666
SWI: Swit_3307
SSAN: NX02_17130
SPHT: K426_15990
MTU: Rv3526(kshA) Rv3571(kshB)
MTC: MT3676
MRA: MRA_3565 MRA_3610(hmp)
MTUR: CFBS_3742 CFBS_3788(hmp)
MTD: UDA_3526 UDA_3571(hmp)
MTUC: J113_24655
MBO: BQ2027_MB3556(ksha) BQ2027_MB3602(kshb)
MBB: BCG_3590 BCG_3636(hmp)
MBT: JTY_3591 JTY_3637(hmp)
MAF: MAF_35380 MAF_35840(hmp)
MUL: MUL_4089 MUL_4142(hmp)
MMI: MMAR_5015 MMAR_5066(hmp)
MPHL: MPHLCCUG_00490(hmp_1) MPHLCCUG_00577(kshA_1) MPHLCCUG_00595(kshA_2) MPHLCCUG_02604(kshA_6) MPHLCCUG_02629(hmp_3)
ASD: AS9A_0920 AS9A_0922(kshA)
RER: RER_07540(kshA) RER_13800(kshA) RER_17750(kshB) RER_51130(kshA)
ROP: ROP_44530(kshA) ROP_58730(kshA2) ROP_58950(kshB) ROP_61150(kshB)
RHB: NY08_2915
RFA: A3L23_01127(hmp_2)
RHS: A3Q41_00422(hmp_1) A3Q41_02260(hmp_2)
GOR: KTR9_0819(kshA) KTR9_3740(kshB) KTR9_5394
SRT: Srot_0411
SLD: T261_3457
SRW: TUE45_04033(hmp_3)
SLX: SLAV_27410(kshA) SLAV_27420(hmp4)
NDK: I601_0574(kshA_1) I601_3442(hmp_2) I601_3444(kshA_2)
AJA: AJAP_26420(kshA) AJAP_26430(kshB)
 » show all
Taxonomy
Reference
1  [PMID:19561185]
  Authors
Petrusma M, Dijkhuizen L, van der Geize R
  Title
Rhodococcus rhodochrous DSM 43269 3-ketosteroid 9alpha-hydroxylase, a two-component iron-sulfur-containing monooxygenase with subtle steroid substrate  specificity.
  Journal
Appl. Environ. Microbiol. 75 (2009) 5300-7.
Reference
2  [PMID:19234303]
  Authors
Capyk JK, D'Angelo I, Strynadka NC, Eltis LD
  Title
Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis.
  Journal
J. Biol. Chem. 284 (2009) 9937-46.
  Sequence
Reference
3  [PMID:21987574]
  Authors
Capyk JK, Casabon I, Gruninger R, Strynadka NC, Eltis LD
  Title
Activity of 3-ketosteroid 9alpha-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis.
  Journal
J. Biol. Chem. 286 (2011) 40717-24.
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.142
IUBMB Enzyme Nomenclature: 1.14.13.142
ExPASy - ENZYME nomenclature database: 1.14.13.142
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.142
BRENDA, the Enzyme Database: 1.14.13.142

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