KEGG   ENZYME: 1.14.14.47Help
Entry
EC 1.14.14.47               Enzyme                                 

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
L-arginine [CPD:C00062];
reduced flavodoxin [CPD:C02745];
O2 [CPD:C00007];
Nomega-hydroxy-L-arginine [CPD:C05933]
Product
L-citrulline [CPD:C00327];
nitric oxide [CPD:C00533];
oxidized flavodoxin [CPD:C02869];
H2O [CPD:C00001];
Nomega-hydroxy-L-arginine [CPD:C05933]
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
ec00220  Arginine biosynthesis
ec00330  Arginine and proline metabolism
ec01100  Metabolic pathways
Orthology
K00491  nitric-oxide synthase, bacterial
Genes
SCL: sce1582(nos)
SCU: SCE1572_10085
SDO: SD1155_11590
BSU: BSU07630(nosA)
BSR: I33_0861
BSL: A7A1_0650
BSH: BSU6051_07630(nosA)
BSY: I653_03830
BSUT: BSUB_00838(nosA)
BSUL: BSUA_00838(nosA)
BSUS: Q433_04305
BSS: BSUW23_03875(nosA)
BST: GYO_1029
BSO: BSNT_07141(yflM)
BSQ: B657_07630(nosA)
BSX: C663_0787
BLI: BL03064(nos)
BLD: BLi00785(nos)
BLH: BaLi_c08860(nosA)
BAY: RBAM_007830(yflM)
BAQ: BACAU_0755(nos)
BYA: BANAU_0700(yflM)
BAMP: B938_03755
BAML: BAM5036_0694(nosA)
BAMA: RBAU_0759(nosA)
BAMN: BASU_0734(nosA)
BAMB: BAPNAU_0711(nos)
BAMT: AJ82_04375
BAMY: V529_07220(yflM)
BMP: NG74_00776(nos)
BAO: BAMF_0731(nos)
BAZ: BAMTA208_03465(nos)
BQL: LL3_00786(nos)
BXH: BAXH7_00731(yflM)
BQY: MUS_0779(nos)
BAMI: KSO_015890
BAMC: U471_07660
BAMF: U722_03910
BHA: BH0823
BAN: BA_5695
BAR: GBAA_5695
BAT: BAS5299
BAH: BAMEG_5743(nos)
BAI: BAA_5726(nos)
BANT: A16_57100
BANR: A16R_57790
BANS: BAPAT_5462
BANV: DJ46_4342(nos)
BCE: BC5444
BCA: BCE_5578
BCZ: BCE33L5141(nos)
BCR: BCAH187_A5626(nos)
BCG: BCG9842_B5379(nos)
BCQ: BCQ_5288(nos)
BCX: BCA_5597(nos)
BAL: BACI_c54380(nos)
BNC: BCN_5370
BCF: bcf_27340
BCER: BCK_08130
BTK: BT9727_5126(nos)
BTL: BALH_4953(nos)
BTB: BMB171_C5040(nos)
BTT: HD73_5859
BTHI: BTK_28880
BTC: CT43_CH5486(nos)
BTM: MC28_4678
BTG: BTB_c56450(nos)
BTI: BTG_21155
BTW: BF38_1166(nos)
BWW: bwei_4336(nos)
BMYO: BG05_562
BMYC: DJ92_2532(nos)
BCL: ABC1267
BPU: BPUM_0714
BPUM: BW16_03800
BPUS: UP12_03895
BPF: BpOF4_10365(nos)
BMQ: BMQ_0362(nos)
BMD: BMD_0363(nos)
BMH: BMWSH_4868(nos)
BMEG: BG04_2652(nos)
BJS: MY9_0854
BACW: QR42_03710
BACP: SB24_05980
BACB: OY17_06555
BACY: QF06_02710
BACL: BS34A_08610(nosA)
BALM: BsLM_0801
BEO: BEH_02605
BGY: BGLY_0801(nos)
BKW: BkAM31D_03290(nos)
BBEV: BBEV_2376(nos)
OIH: OB2691
GKA: GK1676
GGH: GHH_c16880(nos)
GEA: GARCT_01674(nos)
AFL: Aflv_0298
ANM: GFC28_2167(nos)
AAMY: GFC30_793(nos)
ANL: GFC29_3269(nos)
LSP: Bsph_0728
HHD: HBHAL_1332(nos)
HLI: HLI_09830
VPN: A21D_02524(nos)
BSE: Bsel_2946
SAU: SA1730
SAV: SAV1914
SAW: SAHV_1899
SAM: MW1855
SAS: SAS1838
SAR: SAR2007
SAC: SACOL1976
SAE: NWMN_1852
SAD: SAAV_1981
SUE: SAOV_2017
SUZ: MS7_1949(nos)
SUG: SAPIG2009
SAUA: SAAG_02434
SAUE: RSAU_001801(nos)
SAUS: SA40_1755
SAUU: SA957_1839
SAUG: SA268_1911
SAUV: SAI7S6_1014530(nos)
SAUW: SAI5S5_1014470(nos)
SAUX: SAI6T6_1014490(nos)
SAUY: SAI8T7_1014510(nos)
SAUF: X998_1969
SAB: SAB1851
SAUB: C248_1990
SAUC: CA347_2003(nos)
SAUR: SABB_02339(nos)
SAUI: AZ30_10205
SAUD: CH52_09350
SEP: SE1598
SER: SERP1451
SEPP: SEB_01584
SEPS: DP17_542(nos)
SHA: SH1038
SSP: SSP0877
SCA: SCA_1487(nos)
SDT: SPSE_0828(nos)
SPAS: STP1_0432
SXO: SXYL_00923(nos)
SHU: SHYC_04255(nos)
SCAP: AYP1020_1191(nos)
SSCH: LH95_04145
SSCZ: RN70_04365
SAGQ: EP23_05735
MCL: MCCL_1651
MCAK: MCCS_21100(nos)
ESI: Exig_0344
EAN: Eab7_0319(nos)
BBE: BBR47_57280(nos)
PPY: PPE_04584
PPM: PPSC2_23875(nos)
PPO: PPM_4742(nos)
PPOL: X809_40430
PPOY: RE92_13380
PLV: ERIC2_c17570(nos)
PSWU: SY83_12360
AAC: Aaci_2338
AAD: TC41_2620(nos)
SIV: SSIL_3667
JEO: JMA_12200
KZO: NCTC404_00623(nos)
RHA: RHA1_ro02793(nos)
RER: RER_13870(nos)
REY: O5Y_06535
ROP: ROP_24100(nos)
SMA: SAVERM_1531(nos)
SCB: SCAB_31841(txtD)
SVE: SVEN_6572
STRD: NI25_07315
SLX: SLAV_32220(nos)
SRO: Sros_2358
NML: Namu_4253
SEN: SACE_5845(nos) SACE_7255(nos)
SACC: EYD13_10075(nos)
AMD: AMED_4154(nos)
AMN: RAM_21160
AMM: AMES_4106(nos)
AMZ: B737_4106(nos)
AOI: AORI_5274(nos)
PDX: Psed_6636
PSEA: WY02_16105
PSEE: FRP1_26655
PSEH: XF36_27440
AMI: Amir_1303
SESP: BN6_15480 BN6_84360(nos)
AHG: AHOG_18745(nos1) AHOG_27320(nos2)
SAQ: Sare_3563
ASE: ACPL_7469(nos)
ACTN: L083_4136(nos)
AFS: AFR_37445
ACTS: ACWT_7339
CAI: Caci_1733
DRA: DR_2597
DGE: Dgeo_0268
DGO: DGo_CA2502(nos)
CPRV: CYPRO_2999
NPH: NP_1908A(nos)
 » show all
Taxonomy
Reference
1  [PMID:12220171]
  Authors
Pant K, Bilwes AM, Adak S, Stuehr DJ, Crane BR
  Title
Structure of a nitric oxide synthase heme protein from Bacillus subtilis.
  Journal
Biochemistry 41:11071-9 (2002)
DOI:10.1021/bi0263715
  Sequence
[bsu:BSU07630]
Reference
2  [PMID:11856757]
  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
J Biol Chem 277:16167-71 (2002)
DOI:10.1074/jbc.M201136200
Reference
3  [PMID:17127770]
  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
J Biol Chem 282:2196-202 (2007)
DOI:10.1074/jbc.M608206200
Reference
4  [PMID:19805284]
  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
Proc Natl Acad Sci U S A 106:16221-6 (2009)
DOI:10.1073/pnas.0908443106
Reference
5  [PMID:25194416]
  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
J Biol Chem 289:29437-45 (2014)
DOI:10.1074/jbc.M114.595165
  Sequence
[bsu:BSU07630]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.47
IUBMB Enzyme Nomenclature: 1.14.14.47
ExPASy - ENZYME nomenclature database: 1.14.14.47
BRENDA, the Enzyme Database: 1.14.14.47

DBGET integrated database retrieval system