KEGG   ENZYME: 1.18.1.3Help
Entry
EC 1.18.1.3                 Enzyme                                 

Name
ferredoxin---NAD+ reductase;
ferredoxin-nicotinamide adenine dinucleotide reductase;
ferredoxin reductase (ambiguous);
NAD+-ferredoxin reductase;
NADH-ferredoxin oxidoreductase;
reductase, reduced nicotinamide adenine dinucleotide-ferredoxin;
ferredoxin-NAD+ reductase;
NADH-ferredoxin reductase;
NADH2-ferredoxin oxidoreductase;
NADH flavodoxin oxidoreductase;
NADH-ferredoxin NAP reductase (component of naphthalene dioxygenase multicomponent enzyme system);
ferredoxin-linked NAD+ reductase;
NADH-ferredoxin TOL reductase (component of toluene dioxygenase);
ferredoxin---NAD reductase
Class
Oxidoreductases;
Acting on iron-sulfur proteins as donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
ferredoxin:NAD+ oxidoreductase
Reaction(IUBMB)
(1) 2 reduced [2Fe-2S] ferredoxin + NAD+ + H+ = 2 oxidized [2Fe-2S] ferredoxin + NADH [RN:R05875];
(2) reduced 2[4Fe-4S] ferredoxin + NAD+ + H+ = oxidized 2[4Fe-4S] ferredoxin + NADH
Reaction(KEGG)
R05875;
(other) R02000
Show
Substrate
reduced [2Fe-2S] ferredoxin;
NAD+ [CPD:C00003];
H+ [CPD:C00080];
reduced 2[4Fe-4S] ferredoxin
Product
oxidized [2Fe-2S] ferredoxin;
NADH [CPD:C00004];
oxidized 2[4Fe-4S] ferredoxin
Comment
Contains FAD. Reaction (1) is written for a [2Fe-2S] ferredoxin, which is characteristic of some mono- and dioxygenase systems. The alternative reaction (2) is written for a 2[4Fe-4S] ferredoxin, which transfers two electrons, and occurs in metabolism of anaerobic bacteria.
Pathway
Fatty acid metabolism
Xylene degradation
Orthology
K00529  
ferredoxin--NAD+ reductase
K14581  
naphthalene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component
K15758  
xylene monooxygenase electron transfer component
K15765  
toluene monooxygenase electron transfer component
Genes
ECO: 
b2542(hcaD)
ECJ: 
Y75_p2495(hcaD)
ECD: 
EBW: 
BWG_2306(hcaD)
ECE: 
Z3814(hcaD)
ECS: 
ECF: 
ETW: 
ECSP_3486(hcaD)
ELX: 
EOJ: 
EOI: 
EOH: 
EOK: 
ELR: 
ECX: 
ECW: 
ECM: 
ECY: 
ECK: 
ECT: 
EOC: 
CE10_2974(hcaD)
EUM: 
ELO: 
ELH: 
ESO: 
ESM: 
ESL: 
ECL: 
EBR: 
ECB_02434(hcaD)
EBD: 
EKO: 
EKF: 
EDH: 
EDJ: 
EUN: 
ELW: 
ECW_m2768(hcaD)
ELL: 
WFL_13555(hcaD)
ELP: 
EBE: 
B21_02398(hcaD)
SFV: 
SFV_2590(hcaD)
SFE: 
SFxv_2845(hcaD)
SSN: 
SSON_2624(hcaD)
SSJ: 
PLU: 
PAY: 
PAU_02352(hcaD)
ENC: 
EAE: 
KPN: 
KPM: 
SPE: 
PSI: 
XCV: 
XAX: 
PSD: 
FAU: 
VEJ: 
VFU: 
PPF: 
PPX: 
T1E_4244(xylA) T1E_4247(camA) T1E_4269(tobA)
PFS: 
PEN: 
PSC: 
ACI: 
ACD: 
ACB: 
ABY: 
ABC: 
ABN: 
ABB: 
ABX: 
ABZ: 
ABR: 
MAQ: 
MBS: 
GAG: 
CYQ: 
CSA: 
ABO: 
GPB: 
RSC: 
RSL: 
RSN: 
RPI: 
RPF: 
REU: 
REH: 
H16_A1630(h16_A1630) H16_B0802
RME: 
CNC: 
BMA: 
BMV: 
BML: 
BMN: 
BPS: 
BPM: 
BPL: 
BPD: 
BPZ: 
BPQ: 
BTE: 
BVI: 
BUR: 
BCN: 
BCH: 
BCM: 
BCJ: 
BAM: 
BAC: 
BMU: 
BMJ: 
BCT: 
BXE: 
BPH: 
BPY: 
BGL: 
BUG: 
BGF: 
BGD: 
BYI: 
BUK: 
BPX: 
BPE: 
BPC: 
BPER: 
BPA: 
BPAR: 
BBR: 
BBM: 
BBH: 
BPT: 
BAV: 
AXY: 
PUT: 
RFR: 
POL: 
PNA: 
AJS: 
VEI: 
DAC: 
DEL: 
VAP: 
VPE: 
MPT: 
CFU: 
CFU_0345(mocF)
LCH: 
AZO: 
DAR: 
MLO: 
MCI: 
MOP: 
PLA: 
SME: 
SMK: 
SMQ: 
SMX: 
SMD: 
RHI: 
SFH: 
ATU: 
ARA: 
AVI: 
AGR: 
RET: 
REC: 
RLE: 
RLT: 
RLG: 
BMF: 
BMB: 
BMC: 
BMS: 
BMT: 
BOV: 
BCS: 
BMR: 
OAN: 
BJA: 
BRA: 
BBT: 
BRS: 
RPA: 
RPB: 
RPC: 
RPD: 
RPE: 
RPT: 
RPX: 
NWI: 
NHA: 
OCA: 
OCG: 
OCO: 
AOL: 
XAU: 
SNO: 
MEX: 
MEA: 
MDI: 
MCH: 
MRD: 
MET: 
MPO: 
MNO: 
BID: 
MSL: 
CCR: 
CCS: 
CAK: 
CSE: 
PZU: 
BSB: 
AEX: 
SIL: 
SIT: 
RSP: 
RSH: 
RSQ: 
RSK: 
RCP: 
JAN: 
RDE: 
PDE: 
DSH: 
KVU: 
KVL: 
MMR: 
HNE: 
HBA: 
NAR: 
NPP: 
SAL: 
SWI: 
SJP: 
ELI: 
AMV: 
AZL: 
ALI: 
ABS: 
TMO: 
TMO_a0555(thcD)
PBR: 
APB: 
PGV: 
BTS: 
MTF: 
MTB: 
MBT: 
MVA: 
MGI: 
MAB: 
MMC: 
MKM: 
MJL: 
MMI: 
ASD: 
NFA: 
RHA: 
RER: 
ROP: 
ART: 
AAU: 
MLU: 
NCA: 
SRO: 
FRA: 
FRI: 
FAL: 
ACE: 
NML: 
SEN: 
SACE_2839(fprC) SACE_3145(fprC) SACE_3433 SACE_4511(fprC) SACE_5609(padAd2)
AMD: 
AMN: 
AMM: 
PDX: 
CAI: 
RXY: 
RSI: 
CAO: 
CLY: 
PHM: 
AVA: 
CCH: 
TRO: 
HMA: 
HWA: 
NPH: 
 » show all
Taxonomy
Reference
1  [PMID:4147457]
  Authors
Jungermann K, Thauer RK, Leimenstoll G, Decker K.
  Title
Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia.
  Journal
Biochim. Biophys. Acta. 305 (1973) 268-80.
  Organism
Clostridium butyricum, Clostridium pasteurianum
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 (1990) 457-64.
Reference
3  [PMID:1938912]
  Authors
Ramachandra M, Seetharam R, Emptage MH, Sariaslani FS
  Title
Purification and characterization of a soybean flour-inducible ferredoxin reductase of Streptomyces griseus.
  Journal
J. Bacteriol. 173 (1991) 7106-12.
Reference
4  [PMID:1327782]
  Authors
Shaw JP, Harayama S
  Title
Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2.
  Journal
Eur. J. Biochem. 209 (1992) 51-61.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
39369-37-4

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