KEGG   ENZYME: 1.14.15.30
Entry
EC 1.14.15.30               Enzyme                                 

Name
3-ketosteroid 9alpha-monooxygenase;
KshA;
3-ketosteroid 9alpha-hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
androsta-1,4-diene-3,17-dione,[reduced ferredoxin]:oxygen oxidoreductase (9alpha-hydroxylating)
Reaction(IUBMB)
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O [RN:R09860]
Reaction(KEGG)
R09860
Substrate
androsta-1,4-diene-3,17-dione [CPD:C20144];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
9alpha-hydroxyandrosta-1,4-diene-3,17-dione [CPD:C14909];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001]
Comment
The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It forms a two-component system with a ferredoxin reductase (KshB). The enzyme contains a Rieske-type iron-sulfur center and non-heme iron. 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 1.14.15.30 created 2012 as EC 1.14.13.142, transferred 2018 to EC 1.14.15.30
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
RGL: CS053_01730 CS053_01930
VAF: D1115_22765 D1115_23260
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
PKC: PKB_4313(ksha1) PKB_4319(kshB) PKB_4338(ksha3)
PTN: PTRA_a1005(kshB) PTRA_a2590(kshA)
PNG: PNIG_a1057(kshB) PNIG_a2784(kshA)
AXE: P40_21405
REH: H16_B0643(h16_B0643) H16_B0672(hcaE)
RME: Rmet_0543
CGD: CR3_2920(kshA)
BMAL: DM55_4293
BMAE: DM78_3877
BMAQ: DM76_3245
BMAI: DM57_10905
BMAF: DM51_4883
BMAZ: BM44_4256
BMAB: BM45_3379
BPSE: BDL_4290
BPSM: BBQ_5138
BPSU: BBN_4458
BPSD: BBX_6131
BPK: BBK_6151
BPSH: DR55_4337
BPSA: BBU_5033
BPSO: X996_4235
BUT: X994_6124
BCEN: DM39_3466 DM39_6206(hmp) DM39_6233(kshA)
BCED: DM42_6314(hmp) DM42_6338(kshA)
CABA: SBC2_48790(kshB_1) SBC2_48980(kshA)
ADE: Adeh_0398
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)
MPHL: MPHLCCUG_00490(hmp_1) MPHLCCUG_00577(kshA_1) MPHLCCUG_00595(kshA_2) MPHLCCUG_01926(kshA_4) MPHLCCUG_02604(kshA_6) MPHLCCUG_03747(hmp_4)
MTHN: 4412656_00943(kshA_4) 4412656_00961(hmp_2) 4412656_01450(kshA_5) 4412656_03040(hmp_3) 4412656_03259(kshA_6) 4412656_04042(kshA_8) 4412656_04095(hmp_6)
MHAS: MHAS_00793(kshA_2) MHAS_00844(kshA_3) MHAS_02479(kshA_4) MHAS_02573(kshB) MHAS_03041(kshA_5) MHAS_03182(kshA_7) MHAS_03697(kshA_8) MHAS_03711(kshA_9) MHAS_03780(hmp)
MSAL: DSM43276_00501(hmp_1) DSM43276_03419(kshA_2) DSM43276_03727(hmp_4) DSM43276_04014(kshA_3)
MTER: 4434518_01527(kshA_1) 4434518_03344(kshA_2) 4434518_03494(hmp_1) 4434518_03640(kshA_3) 4434518_03730(hmp_2)
RER: RER_07540(kshA) RER_09150(kshA2) RER_13800(kshA) RER_17750(kshB) RER_51130(kshA)
ROP: ROP_22170(kshA) 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)
RRT: 4535765_00581(kshA_1) 4535765_00622(kshA_2) 4535765_00625(kshB_1) 4535765_03583(hmp_2) 4535765_04053(kshA_4) 4535765_04385(kshB_2)
GRU: GCWB2_04170(kshA1) GCWB2_11625(kshA2) GCWB2_19200(hmp6) GCWB2_21220(hmp7) GCWB2_21605(kshA4)
GOM: D7316_02031(kshA_1) D7316_02407(hmp_2) D7316_02456(kshA_2) D7316_02565(kshA_3) D7316_02584(kshB_1) D7316_03108(kshA_4) D7316_04922(kshB_2)
SRT: Srot_0411
SFI: SFUL_6946
SLD: T261_3457
SRW: TUE45_04033(hmp_3)
SLX: SLAV_27410(kshA) SLAV_27420(hmp4)
LMOI: VV02_06590
NDK: I601_0574(kshA_1) I601_3442(hmp_2) I601_3444(kshA_2)
FAL: FRAAL3502
AJA: AJAP_26420(kshA) AJAP_26430(kshB)
AMYY: YIM_14425(hmp1) YIM_14435(kshA1) YIM_36730(hmp4) YIM_36740(kshA2)
PSL: Psta_0972
GMR: GmarT_59890(ndoA)
MGOT: MgSA37_00351(hmp)
FAE: FAES_0794(paaE)
 » show all
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 75:5300-7 (2009)
DOI:10.1128/AEM.00066-09
  Sequence
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 284:9937-46 (2009)
DOI:10.1074/jbc.M900719200
  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 286:40717-24 (2011)
DOI:10.1074/jbc.M111.289975
Other DBs
ExplorEnz - The Enzyme Database: 1.14.15.30
IUBMB Enzyme Nomenclature: 1.14.15.30
ExPASy - ENZYME nomenclature database: 1.14.15.30
BRENDA, the Enzyme Database: 1.14.15.30
LinkDB

DBGET integrated database retrieval system