KEGG   ORTHOLOGY: K14338
Entry
K14338                      KO                                     
Symbol
cypD_E, CYP102A, CYP505
Name
cytochrome P450 / NADPH-cytochrome P450 reductase [EC:1.14.14.1 1.6.2.4]
Pathway
map00071  Fatty acid degradation
map00380  Tryptophan metabolism
map00627  Aminobenzoate degradation
map01120  Microbial metabolism in diverse environments
Reaction
R03629  melatonin,NADPH---hemoprotein reductase:oxygen oxidoreductase
R04121  fatty acid,reduced-flaboprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
R05259  parathion,NADPH---hemoprotein reductase:oxygen oxidoreductase (paraoxon-forming)
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09103 Lipid metabolism
   00071 Fatty acid degradation
    K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
  09105 Amino acid metabolism
   00380 Tryptophan metabolism
    K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
  09111 Xenobiotics biodegradation and metabolism
   00627 Aminobenzoate degradation
    K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   00199 Cytochrome P450
    K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.6  Acting on NADH or NADPH
   1.6.2  With a heme protein as acceptor
    1.6.2.4  NADPH---hemoprotein reductase
     K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.14  With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.14.1  unspecific monooxygenase
     K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
Cytochrome P450 [BR:ko00199]
 Cytochrome P450, fungi type
  CYP505 family
   K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
 Cytochrome P450, bacteria type
  CYP102 family
   K14338  cypD_E, CYP102A, CYP505; cytochrome P450 / NADPH-cytochrome P450 reductase
Other DBs
COG: COG2124 COG0369
GO: 0070330 0003958
Genes
NCR: NCU05185
NTE: NEUTE1DRAFT145879(NEUTE1DRAFT_145879)
SMP: SMAC_07143
PAN: PODANSg1328 PODANSg2208 PODANSg3804 PODANSg5780
PBEL: QC761_0025340 QC761_110820 QC761_124450 QC761_506770
PPSD: QC762_0088670 QC762_110820 QC762_124450 QC762_506770
PPSP: QC763_110820 QC763_124450 QC763_506770
PPSA: QC764_0086770 QC764_110820 QC764_124450 QC764_506770
TTT: THITE_2144773
MTM: MYCTH_101224
CMT: CCM_02979
MBE: MBM_08168
ABE: ARB_05231
TVE: TRV_02270
ZTR: MYCGRDRAFT_100796(CYP-40) MYCGRDRAFT_70343(CYP-50)
CCAC: CcaHIS019_0500810(ISA1)
HIR: HETIRDRAFT_124013(cpr1)
PCT: PC1_0268
XAG: HEP73_00655(cypB)
XAS: HEP74_00630(cypB)
RPI: Rpic_4258
REH: H16_B1009(h16_B1009)
CNC: CNE_2c09660(cypE)
RME: Rmet_3467
BCEO: I35_5939
BCED: DM42_5902
BCON: NL30_31780
BPSL: WS57_03680
BJA: blr2882(blr2882)
BRS: S23_51340
BRAD: BF49_1812
BARH: WN72_15805
BVZ: BRAD3257_5827(cypD)
RPB: RPB_3645
RPD: RPD_1820
VGO: GJW-30_1_03917(cypE)
TALZ: RPMA_20310
ELI: ELI_00100
BSU: BSU07250(yetO) BSU27160(cypB)
BSH: BSU6051_07250(yetO) BSU6051_27160(cypB)
BSUT: BSUB_00799(yetO) BSUB_02898(cypB)
BSUL: BSUA_00799(yetO) BSUA_02898(cypB)
BSQ: B657_07250(cypD) B657_27160(cypB)
BSX: C663_0751(cypD) C663_2550(cypE)
BSS: BSUW23_03690(cypD) BSUW23_13125(cypB)
BLI: BL02398(cypE)
BLD: BLi02848(yrhJ)
BLH: BaLi_c29470(cypB)
BAQ: BACAU_0708(yetO) BACAU_2438(yrhJ)
BYA: BANAU_0661(yetO) BANAU_2583(yrhJ)
BQY: MUS_0726(yetO) MUS_2901(yrhJ)
BAML: BAM5036_0659(cypD) BAM5036_2365(cypB)
BAMA: RBAU_0722(cypD) RBAU_2563(cypB)
BAMN: BASU_0699(cypD) BASU_2369(cypB)
BAMB: BAPNAU_0670(YetO) BAPNAU_1137(yrhJ)
BAMY: V529_06850(yetO) V529_27090(yrhJ)
BAO: BAMF_0695(yetO) BAMF_2522(cypB)
BAZ: BAMTA208_03280(yetO) BAMTA208_13325(cypB)
BQL: LL3_00745(yetO) LL3_02800(yrhJ)
BXH: BAXH7_00690(yetO) BAXH7_02724(yrhJ)
BMOJ: HC660_07720(cypD) HC660_25190(cypB)
BSTR: QI003_04010(cypD) QI003_16740(cypB)
BAN: BA_3221(cypD)
BAR: GBAA_3221(cypD)
BAT: BAS2993
BAH: BAMEG_1392(cypD)
BAI: BAA_3269(cypD)
BANT: A16_32460
BANR: A16R_32890
BANS: BAPAT_3089
BANV: DJ46_1971(cyp102A1)
BCE: BC3211
BCA: BCE_3239(cypD)
BCR: BCAH187_A3250(cypD)
BCB: BCB4264_A3231(cypD)
BCU: BCAH820_3229(cypD)
BCG: BCG9842_B2016(cypD)
BCQ: BCQ_3034(cypD)
BCX: BCA_3251(cypD)
BNC: BCN_3047
BCF: bcf_15685
BCER: BCK_18985
BTL: BALH_2868
BTB: BMB171_C2898(cypD)
BTT: HD73_2783
BTHI: BTK_13800
BTC: CT43_CH3164(cypD)
BTM: MC28_2359
BTG: BTB_c32980(cypD)
BTI: BTG_03315
BTW: BF38_4372(cyp102A1)
BWW: bwei_1841(cypD)
BMYC: DJ92_5480(cyp102A1)
BTRO: FJR70_03215(cypD)
BNT: GSN03_15235(cypD)
BPAC: LMD38_11060(cypD)
BPAN: NLJ82_15170(cypD)
BALU: QRY64_18325(cypD)
BPU: BPUM_1680
BPUM: BW16_09260
BPUS: UP12_08650
BGY: BGLY_3163
BAER: BAE_16285
BCAB: EFK13_04180(cypD) EFK13_13775(cypB)
BRY: M0696_13560(cypB)
BACW: QR42_08590
BACL: BS34A_08250(yetO) BS34A_29630(cypB)
BMQ: BMQ_3237
BMD: BMD_3248
BMH: BMWSH_1945(cypD)
BMEG: BG04_163(cYP102a1)
BEO: BEH_16435
PPO: PPM_3514(M1_3883)
PPOL: X809_33460
PPQ: PPSQR21_035110(cysJ)
PPOY: RE92_19680
PMS: KNP414_03453(cypD)
PMW: B2K_06870
PSWU: SY83_13600
ASOC: CB4_02158(cypE)
MMAN: MMAN_56760
MCOO: MCOO_15200
MIJ: MINS_17710(cypD)
MALV: MALV_48980
MGAD: MGAD_23110
MAUB: MAUB_44070
MPOF: MPOR_04230
MPHU: MPHO_25300
MBOK: MBOE_27830
MCHE: BB28_22565
MSTE: MSTE_04573
MMIN: MMIN_05950
MHIB: MHIB_23090
SMA: SAVERM_575(cyp2)
SCB: SCAB_5931
SHY: SHJG_8055
SDV: BN159_1745(cypD)
STRE: GZL_01897
SLD: T261_1104
STRM: M444_30060
SLE: sle_05650(sle_05650)
SALU: DC74_6871
SALL: SAZ_35695
SALJ: SMD11_0205(cypD_E)
SCYG: S1361_31690(cypE)
SAUH: SU9_029790
SNIG: HEK616_44710(cypB)
SCT: SCAT_4838(CYP102A)
SRO: Sros_6421
NCX: Nocox_24955(cypE)
SEN: SACE_4205(cypD)
PDX: Psed_5892
PSEE: FRP1_10540
KAL: KALB_657
HAU: Haur_2522
DGO: DGo_PB0521(cypD)
SACI: Sinac_6636
PBOR: BSF38_00176(cypB)
SGN: SGRA_1002
 » show all
Reference
PMID:9141694
  Authors
Yamamoto H, Uchiyama S, Nugroho FA, Sekiguchi J
  Title
A 23.4 kb segment at the 69 degrees-70 degrees region of the Bacillus subtilis genome.
  Journal
Microbiology 143 ( Pt 4):1317-20 (1997)
DOI:10.1099/00221287-143-4-1317
  Sequence
[bsu:BSU07250]
Reference
  Authors
Gustafsson MC, Roitel O, Marshall KR, Noble MA, Chapman SK, Pessegueiro A, Fulco AJ, Cheesman MR, von Wachenfeldt C, Munro AW
  Title
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
  Journal
Biochemistry 43:5474-87 (2004)
DOI:10.1021/bi035904m
Reference
PMID:11985584 (CYP505)
  Authors
Kitazume T, Tanaka A, Takaya N, Nakamura A, Matsuyama S, Suzuki T, Shoun H
  Title
Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system.
  Journal
Eur J Biochem 269:2075-82 (2002)
DOI:10.1046/j.1432-1033.2002.02855.x
  Sequence

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