KEGG   ENZYME: 1.18.1.6Help
Entry
EC 1.18.1.6                 Enzyme                                 

Name
adrenodoxin-NADP+ reductase;
adrenodoxin reductase;
nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase;
AdR;
NADPH:adrenal ferredoxin oxidoreductase;
NADPH-adrenodoxin reductase
Class
Oxidoreductases;
Acting on iron-sulfur proteins as donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
reduced adrenodoxin:NADP+ oxidoreductase
Reaction(IUBMB)
2 reduced adrenodoxin + NADP+ + H+ = 2 oxidized adrenodoxin + NADPH [RN:R10159]
Reaction(KEGG)
Substrate
reduced adrenodoxin [CPD:C00662];
NADP+ [CPD:C00006];
H+ [CPD:C00080]
Product
oxidized adrenodoxin [CPD:C00667];
NADPH [CPD:C00005]
Comment
A flavoprotein (FAD). The enzyme, which transfers electrons from NADPH to adrenodoxin molecules, is the first component of the mitochondrial cytochrome P-450 electron transfer systems, and is involved in the biosynthesis of all steroid hormones.
History
EC 1.18.1.6 created 1965 as EC 1.6.99.4, transferred 1972 as EC 1.6.7.1, transferred 1978 to EC 1.18.1.2, part transferred 2012 to EC 1.18.1.6, modified 2016
Orthology
K18914  adrenodoxin-NADP+ reductase
Genes
HSA: 2232(FDXR)
PTR: 454869(FDXR)
PPS: 100974527(FDXR)
GGO: 101147693(FDXR)
PON: 100437093(FDXR)
NLE: 100604648(FDXR)
MCC: 699336(FDXR)
MCF: 102137303(FDXR)
CSAB: 103243070(FDXR)
RRO: 104681334(FDXR)
RBB: 108537405(FDXR)
CJC: 100385090(FDXR)
SBQ: 101045800(FDXR)
MMU: 14149(Fdxr)
RNO: 79122(Fdxr)
CGE: 100773278(Fdxr)
NGI: 103732755(Fdxr)
HGL: 101700719(Fdxr)
CCAN: 109687573(Fdxr)
OCU: 103346270(FDXR)
TUP: 102478703(FDXR)
CFA: 475910(FDXR)
AML: 100475805(FDXR)
UMR: 103665719(FDXR)
ORO: 101368875(FDXR)
FCA: 101096022(FDXR)
PTG: 102959508(FDXR)
AJU: 106987731(FDXR)
BTA: 282604(FDXR)
BOM: 102273000(FDXR)
BIU: 109574321(FDXR)
PHD: 102341267(FDXR)
CHX: 102174063(FDXR)
OAS: 101111818(FDXR)
SSC: 100512919(FDXR)
CFR: 102519985(FDXR)
CDK: 105104618(FDXR)
BACU: 103000856(FDXR)
LVE: 103086167(FDXR)
OOR: 101286717(FDXR)
ECB: 100060312(FDXR)
EPZ: 103546558(FDXR)
EAI: 106830270(FDXR)
MYB: 102263706(FDXR)
MYD: 102766204(FDXR)
HAI: 109383628(FDXR)
RSS: 109454732(FDXR)
PALE: 102883561(FDXR)
LAV: 100655948(FDXR)
TMU: 101340285
MDO: 100027953(FDXR)
SHR: 100922569(FDXR)
OAA: 100083234(FDXR)
GGA: 769635(FDXR)
MGP: 100540404(FDXR)
CJO: 107322365(FDXR)
APLA: 101800804(FDXR)
ACYG: 106034619(FDXR)
TGU: 100220739(FDXR)
GFR: 102034179(FDXR)
FAB: 101817164(FDXR)
PHI: 102103074(FDXR)
PMAJ: 107212633(FDXR)
CCW: 104694370(FDXR)
FPG: 101910552(FDXR)
FCH: 102046860(FDXR)
CLV: 102085677(FDXR)
EGZ: 104125332(FDXR)
ASN: 102373045(FDXR)
AMJ: 102563408(FDXR)
PSS: 102459685(FDXR)
CMY: 102935912(FDXR)
CPIC: 101952957(FDXR)
ACS: 100559841(fdxr)
PVT: 110085820(FDXR)
PBI: 103051603(FDXR)
GJA: 107110041(FDXR)
XLA: 108702801(fdxr.S) 495142(fdxr.L)
XTR: 100158651(fdxr)
NPR: 108797020(FDXR)
DRE: 100536115(fdxr)
SRX: 107711271
SANH: 107667767(fdxr)
SGH: 107567808(fdxr)
CCAR: 109054119(fdxr)
IPU: 108273819(fdxr)
TRU: 101073938(fdxr) 101079042
LCO: 104924915(fdxr) 109137258
MZE: 101468891(fdxr)
OLA: 101160395(fdxr)
XMA: 102233690(fdxr)
PRET: 103481952(fdxr)
NFU: 107388287(fdxr)
CSEM: 103382155(fdxr)
LCF: 108872584(fdxr) 108891381
HCQ: 109513310(fdxr)
BPEC: 110155172(fdxr)
SASA: 106589468(fdxr)
ELS: 105023035(fdxr)
SFM: 108940168(fdxr)
LCM: 102360919(FDXR)
CMK: 103175676(fdxr)
CIN: 100177510
SPU: 585224
APLC: 110979675
SKO: 100373097
DME: Dmel_CG12390(dare)
DSI: Dsimw501_GD15255(Dsim_GD15255)
MDE: 101888739
AAG: 5568320
AME: 100578109
BIM: 100742822
BTER: 100643757
AEC: 105148416
ACEP: 105619099
PBAR: 105433423
HST: 109503578
CFO: 105259167
PGC: 109852590
NVI: 100118934
TCA: 658878
DPA: 109543924
NVL: 108559754
BMOR: 101736047
PMAC: 106720445
PRAP: 110993775
PXY: 105386739
API: 100163608
DNX: 107162313
ZNE: 110840377
FCD: 110859784
TUT: 107367827
CEL: CELE_Y62E10A.6(Y62E10A.6)
CBR: CBG01781
BMY: Bm1_54850
TSP: Tsp_06076
CRG: 105329622
MYI: 110450206
OBI: 106882139
LAK: 106177774
SHX: MS3_05698
EPA: 110242963
HMG: 100200068
AQU: 100637039
ATH: AT4G32360
CRB: 17880727
BRP: 103864869
BOE: 106318680
THJ: 104799066
CPAP: 110818598
CIT: 102628424
TCC: 18588561
GRA: 105787215
EGR: 104438256
VRA: 106765554
VAR: 108346262
CCAJ: 109804194
CAM: 101500867
LJA: Lj4g3v3060470.1(Lj4g3v3060470.1) Lj4g3v3060470.2(Lj4g3v3060470.2)
ADU: 107478608
AIP: 107630280
LANG: 109349811
PPER: 18770919
PMUM: 103340886
CSV: 101208191
CMO: 103483451
MCHA: 111016072
CMAX: 111479698
CMOS: 111432190
CPEP: 111790949
RCU: 8262557
JCU: 105637751
HBR: 110664984
VVI: 100252665
SLY: 101245589
SPEN: 107008435
SOT: 102598661
CANN: 107839770
NSY: 104228460
NTO: 104098479
INI: 109153160
SIND: 105168712
OEU: 111398852
HAN: 110928552
LSV: 111883878
DCR: 108214615
BVG: 104902247
SOE: 110799347
NNU: 104595144
OSA: 4329009
DOSA: Os02t0277600-01(Os02g0277600)
OBR: 102699565
BDI: 100845899
ATS: 109777158(LOC109777158)
SBI: 8060381
ZMA: 100285690(pco114328(55)) 109946101 109946102
PDA: 103702547
EGU: 105040853
MUS: 103987769
DCT: 110095192
ATR: 18426683
PPP: 112287080
CRE: CHLREDRAFT_134840(ARH1)
MNG: MNEG_2646
APRO: F751_5995
SCE: YDR376W(ARH1)
ERC: Ecym_4641
KMX: KLMA_20603(ARH1)
NCS: NCAS_0A11790(NCAS0A11790)
NDI: NDAI_0A04500(NDAI0A04500)
TPF: TPHA_0E01640(TPHA0E01640)
TBL: TBLA_0A02700(TBLA0A02700)
TDL: TDEL_0D02510(TDEL0D02510)
KAF: KAFR_0E03780(KAFR0E03780)
PIC: PICST_52035(ARH1)
CAL: CAALFM_C204880CA(ARH2)
CAUR: QG37_07776
SLB: AWJ20_604(ARH1)
NCR: NCU08005
MGR: MGG_14814
MAW: MAC_07893
MAJ: MAA_05280
CMT: CCM_02929
BFU: BCIN_15g03520(Bcarh1)
MBE: MBM_04149
ANI: AN6272.2
ANG: ANI_1_2280024(An02g01540)
ABE: ARB_04864
TVE: TRV_06564
PTE: PTT_11539
SPO: SPBC3B8.01c(arh1)
CNE: CNL05820
CNB: CNBI1010
LBC: LACBIDRAFT_305530(LbAdr1)
ABP: AGABI1DRAFT77612(AGABI1DRAFT_77612)
ABV: AGABI2DRAFT212328(AGABI2DRAFT_212328)
MGL: MGL_1519
DDI: DDB_G0287353(fdxr)
DFA: DFA_07524(fdxr)
PYO: PY17X_0910700(PY02070)
PCB: PCHAS_071060(PC000605.01.0)
TAN: TA15585
TPV: TP02_0869
BBO: BBOV_I000680(16.m00963)
CPV: cgd8_2710
SMIN: v1.2.025356.t1(symbB.v1.2.025356.t1)
SPAR: SPRG_05062
 » show all
Taxonomy
Reference
1
  Authors
Omura, T., Sanders, E., Estabrook, R.W., Cooper, D.Y. and Rosenthal, O.
  Title
Isolation from adrenal cortex of a nonheme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P-450 reductase.
  Journal
Arch Biochem Biophys 117:660-673 (1966)
Reference
2  [PMID:4144106]
  Authors
Chu JW, Kimura T
  Title
Studies on adrenal steroid hydroxylases. Molecular and catalytic properties of adrenodoxin reductase (a flavoprotein).
  Journal
J Biol Chem 248:2089-94 (1973)
Reference
3  [PMID:235468]
  Authors
Sugiyama T, Yamano T
  Title
Purification and crystallization of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria.
  Journal
FEBS Lett 52:145-8 (1975)
DOI:10.1016/0014-5793(75)80658-2
Reference
4  [PMID:6766943]
  Authors
Hanukoglu I, Jefcoate CR.
  Title
Mitochondrial cytochrome P-450sec. Mechanism of electron transport by adrenodoxin.
  Journal
J Biol Chem 255:3057-61 (1980)
Reference
5  [PMID:3011431]
  Authors
Hanukoglu I, Hanukoglu Z
  Title
Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase in adrenal cortex and corpus luteum. Implications for membrane organization and gene regulation.
  Journal
Eur J Biochem 157:27-31 (1986)
DOI:10.1111/j.1432-1033.1986.tb09633.x
Reference
6  [PMID:2924777]
  Authors
Hanukoglu I, Gutfinger T
  Title
cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases.
  Journal
Eur J Biochem 180:479-84 (1989)
DOI:10.1111/j.1432-1033.1989.tb14671.x
  Sequence
[bta:282604]
Reference
7  [PMID:10369776]
  Authors
Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE
  Title
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis.
  Journal
J Mol Biol 289:981-90 (1999)
DOI:10.1006/jmbi.1999.2807
  Sequence
[bta:282604]
Other DBs
ExplorEnz - The Enzyme Database: 1.18.1.6
IUBMB Enzyme Nomenclature: 1.18.1.6
ExPASy - ENZYME nomenclature database: 1.18.1.6
BRENDA, the Enzyme Database: 1.18.1.6

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