Entry
Name
nitric-oxide synthase (flavodoxin);
nitric oxide synthetase (ambiguous);
NO synthase (ambiguous)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
L-arginine,reduced-flavodoxin:oxygen oxidoreductase (nitric-oxide-forming)
Reaction(IUBMB)
2 L-arginine + 3 reduced flavodoxin + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O (overall reaction) [RN:
R11711 ];
(1a) 2 L-arginine + 2 reduced flavodoxin + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O [RN:
R11712 ];
(1b) 2 Nomega-hydroxy-L-arginine + reduced flavodoxin + 2 O2 = 2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O [RN:
R11713 ]
Reaction(KEGG)
Substrate
Product
Comment
Binds heme (iron protoporphyrin IX) and tetrahydrobiopterin. The enzyme, found in bacteria and archaea, consist of only an oxygenase domain and functions together with bacterial ferredoxins or flavodoxins. The orthologous enzymes from plants and animals also contain a reductase domain and use only NADPH as the electron donor (cf. EC
1.14.13.39 ).
History
EC 1.14.14.47 created 2012 as EC 1.14.13.165, transferred 2017 to EC 1.14.14.47
Pathway
ec00330 Arginine and proline metabolism
Orthology
K00491 nitric-oxide synthase, bacterial
Genes
SAUV : SAI7S6_1014530(nos)
SAUW : SAI5S5_1014470(nos)
SAUX : SAI6T6_1014490(nos)
SAUY : SAI8T7_1014510(nos)
SDP : NCTC12225_00897(nos)
SPIC : SAMEA4384060_1034(nos)
SSH : NCTC13712_01935(nos)
SSIM : SAMEA4384339_1835(nos)
SSTE : SAMEA4384403_0769(nos)
LGZ : NCTC10812_01779(nos)
NAD : NCTC11293_00971(nos)
NGP : LTT66_13825 LTT66_14690
NSPU : IFM12276_66180(nos)
STRM : M444_05170 M444_06580
SVR : CP971_05395 CP971_07990
SXT : KPP03845_101240(nos)
SGK : PET44_03740 PET44_05155
STRH : GXP74_23250 GXP74_38950
NOA : BKM31_09450 BKM31_32400
NGN : LCN96_12835 LCN96_31860
SEN : SACE_5845(nos) SACE_7255(nos)
SESP : BN6_15480 BN6_84360(nos)
SSYI : EKG83_07520 EKG83_46180
KUT : JJ691_78600(nos_1) JJ691_96290(nos_2)
KPHY : AOZ06_05175 AOZ06_41055 AOZ06_46845 AOZ06_51945 AOZ06_52570
LED : BBK82_02920 BBK82_14965
AHM : TL08_17805 TL08_26260
ACTI : UA75_21735 UA75_30065
ACAD : UA74_21255 UA74_29535
AHG : AHOG_18745(nos1) AHOG_27320(nos2)
CROS : N8J89_29195 N8J89_32180 N8J89_41205
ACTY : OG774_06880 OG774_15505
UME : RM788_24695 RM788_35305
ACTR : Asp14428_16080 Asp14428_59460(nos)
PRY : Prubr_36930(nos) Prubr_37480
DROS : Drose_14845 Drose_30495
» show all
Taxonomy
Reference
Authors
Pant K, Bilwes AM, Adak S, Stuehr DJ, Crane BR
Title
Structure of a nitric oxide synthase heme protein from Bacillus subtilis.
Journal
Sequence
Reference
Authors
Adak S, Aulak KS, Stuehr DJ
Title
Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis.
Journal
Reference
Authors
Wang ZQ, Lawson RJ, Buddha MR, Wei CC, Crane BR, Munro AW, Stuehr DJ
Title
Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.
Journal
Reference
Authors
Agapie T, Suseno S, Woodward JJ, Stoll S, Britt RD, Marletta MA
Title
NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum.
Journal
Reference
Authors
Holden JK, Lim N, Poulos TL
Title
Identification of redox partners and development of a novel chimeric bacterial nitric oxide synthase for structure activity analyses.
Journal
Sequence
Other DBs