KEGG   ENZYME: 1.18.1.7
Entry
EC 1.18.1.7                 Enzyme                                 
Name
ferredoxin---NAD(P)+ reductase (naphthalene dioxygenase ferredoxin-specific);
NADH-ferredoxin(NAP) reductase
Class
Oxidoreductases;
Acting on iron-sulfur proteins as donors;
With NAD+ or NADP+ as acceptor
Sysname
ferredoxin:NAD(P)+ oxidoreductase
Reaction(IUBMB)
2 reduced [2Fe-2S] ferredoxin + NAD(P)+ + H+ = 2 oxidized [2Fe-2S] ferredoxin + NAD(P)H [RN:R05875 R12422]
Reaction(KEGG)
R05875 R12422
Substrate
reduced [2Fe-2S] ferredoxin [CPD:C22150];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H+ [CPD:C00080]
Product
oxidized [2Fe-2S] ferredoxin [CPD:C22151];
NADH [CPD:C00004];
NADPH [CPD:C00005]
Comment
The enzyme from the aerobic bacterium Ralstonia sp. U2 donates electrons to both EC 1.14.12.12, naphthalene 1,2-dioxygenase and EC 1.14.13.172, salicylate 5-hydroxylase [1]. The enzyme from Pseudomonas NCIB 9816 is specific for the ferredoxin associated with naphthalene dioxygenase; it contains FAD and a [2Fe-2S] cluster.
History
EC 1.18.1.7 created 2013
Orthology
K14581  naphthalene 1,2-dioxygenase ferredoxin reductase component
Genes
EBTEBL_c34260(ndoR)
KASKATP_22580
KLUK7B04_17400
PPIND053(nahAa)
PFKPFAS1_28600
PSCA458_06735
PSTUUIB01_22615
PBMCL52_14600
ALTambt_18035
MMWMmwyl1_2668
MMEMarme_2403
MPCMar181_2356
MPRIMP3633_2252
FCEJN531_005600
RSORSc1091(nagAa)
RSLRPSI07_2300(ndoR)
RSNRSPO_c02273
RSMCMR15_20210(ndoR)
RSEF504_1062
RSYRSUY_15130
RPJN234_28700
RMNTK49_07925
RPUCDC45_05600
RSGJK151_19130
CBWRR42_s2750
CCUPBKK81_31190
CUPBKK80_25160
CUUBKK79_30870
CCAXKZ686_18760
BMKDM80_1434(ndoR) DM80_1439(ndoR)
BUGBC1001_0575
BUQAC233_10920
BPXBUPH_04465
BUZAYM40_33160
BFNOI25_3043(ndoR)
PARBCJU94_38680
PTERC2L65_39085
PPKU875_04290
PPNODA70_21365
PPNMLV28_08955
PRBX636_05155
PPULRO07_03185
PSPUNA29_24095
PAPISG18_03375
PVEUC34_19340
POXMB84_24095
PFGAB870_06335
PNRAT302_02770
PFIBPI93_008705
PCOMNTU39_21100
AXYAXYL_06582
AFAUZ73_08385
AFQAFA_02200
AAQUD3M96_02175
PIGEGT29_02420 EGT29_23985
POLBpro_0980
PNAPnap_2489
AAVAave_0164
AJSAjs_3089
AAAAcav_0195
ACKC380_10005
VPEVarpa_2932
VBOCKY39_17850
VAMC4F17_05700
JAJEKL02_16445
MASYDPH57_09575
UNDUNDKW_4644
LCHLcho_0800
TINTint_1781
THITHI_2205
AZOazo2517(nagAa)
AOAdqs_2674
AZRCJ010_15890
SIXBSY16_5589
RHVBA939_22370
SHZshn_02370
OANOant_3238 Oant_4051
OAHDR92_3251 DR92_4202
OCRHGK82_13400
OCLGTN27_14640
BOPAXW83_15000
STARG3545_17180
MRDMrad2831_0219
MNOMnod_0136
MPHYMCBMB27_05204
METXA3862_01170
MOCBB934_42075
CDQBOQ54_10960
HMCHYPMC_3092
AALAIGS74_00605
NOHG5V57_28305
RBMTEF_01260
PSFPSE_0864
PPHRAPZ00_10945
LAPACP90_27015
LABRCHH27_20650
LABTFIU93_04780(nagAa1)
LAGGB0E33_11075
SIWGH266_12635
PYEA6J80_03590
PARREOJ32_06500
PKDF8A10_03980
SGISGRAN_2805(thnY)
DVNHQ394_12615
TMOTMO_2240(ndoR)
TIIDY252_20845
ASLAeqsu_1257
 » show all
Reference
1  [PMID:11872705]
  Authors
Zhou NY, Al-Dulayymi J, Baird MS, Williams PA
  Title
Salicylate 5-hydroxylase from Ralstonia sp. strain U2: a monooxygenase with close relationships to and shared electron transport proteins with naphthalene dioxygenase.
  Journal
J Bacteriol 184:1547-55 (2002)
DOI:10.1128/JB.184.6.1547-1555.2002
  Sequence
Reference
2  [PMID:2294092]
  Authors
Haigler BE, Gibson DT
  Title
Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816.
  Journal
J Bacteriol 172:457-64 (1990)
DOI:10.1128/JB.172.1.457-464.1990
Other DBs
ExplorEnz - The Enzyme Database: 1.18.1.7
IUBMB Enzyme Nomenclature: 1.18.1.7
ExPASy - ENZYME nomenclature database: 1.18.1.7
BRENDA, the Enzyme Database: 1.18.1.7
LinkDB

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