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Protein

Nitric oxide synthase oxygenase

Gene

nos

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the production of nitric oxide.1 Publication

Catalytic activityi

2 L-arginine + 3 NAD(P)H + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H2O.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • heme1 Publication
  • 5,6,7,8-tetrahydrobiopterin1 PublicationNote: Tetrahydrobiopterin (H4B). Can also use tetrahydrofolate (THF) in place of tetrahydrobiopterin (H4B) but binds THF with much lower affinity than H4B.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi66Iron (heme axial ligand)1

GO - Molecular functioni

  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • nitric-oxide synthase activity Source: UniProtKB

GO - Biological processi

  • nitric oxide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciBSUB:BSU07630-MONOMER.
SABIO-RKO34453.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase oxygenase (EC:1.14.13.165)
Alternative name(s):
NOSoxy-like protein
Gene namesi
Name:nos
Synonyms:yflM
Ordered Locus Names:BSU07630
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709531 – 363Nitric oxide synthase oxygenaseAdd BLAST363

Proteomic databases

PaxDbiO34453.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004263.

Chemistry databases

BindingDBiO34453.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 21Combined sources19
Helixi25 – 27Combined sources3
Helixi28 – 42Combined sources15
Helixi49 – 61Combined sources13
Helixi69 – 74Combined sources6
Beta strandi76 – 79Combined sources4
Helixi86 – 101Combined sources16
Helixi102 – 104Combined sources3
Beta strandi109 – 112Combined sources4
Beta strandi117 – 119Combined sources3
Beta strandi122 – 125Combined sources4
Beta strandi128 – 131Combined sources4
Beta strandi135 – 138Combined sources4
Beta strandi141 – 144Combined sources4
Helixi146 – 148Combined sources3
Helixi149 – 157Combined sources9
Beta strandi172 – 176Combined sources5
Beta strandi183 – 185Combined sources3
Helixi189 – 191Combined sources3
Beta strandi194 – 196Combined sources3
Helixi203 – 208Combined sources6
Beta strandi211 – 214Combined sources4
Beta strandi222 – 225Combined sources4
Beta strandi228 – 231Combined sources4
Helixi241 – 245Combined sources5
Turni246 – 250Combined sources5
Turni252 – 255Combined sources4
Helixi258 – 264Combined sources7
Helixi272 – 274Combined sources3
Helixi276 – 295Combined sources20
Helixi302 – 319Combined sources18
Helixi327 – 330Combined sources4
Beta strandi333 – 335Combined sources3
Helixi336 – 338Combined sources3
Helixi340 – 343Combined sources4
Beta strandi352 – 356Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7VX-ray1.95A5-363[»]
1M7ZX-ray2.14A5-363[»]
2AMOX-ray2.60A/B30-363[»]
2AN0X-ray2.60A18-363[»]
2AN2X-ray2.60A18-363[»]
2FBZX-ray2.10X5-363[»]
2FC1X-ray2.00A5-363[»]
2FC2X-ray2.20A/B5-363[»]
4D3IX-ray2.09A1-363[»]
4D3JX-ray1.67A1-363[»]
4D3KX-ray2.02A/B1-363[»]
4D3MX-ray1.74A1-363[»]
4D3NX-ray2.13A1-363[»]
4D3OX-ray1.90A1-363[»]
4D3TX-ray1.55A1-363[»]
4D3UX-ray1.98A1-363[»]
4D3VX-ray1.88A1-363[»]
4D7HX-ray2.02A1-363[»]
4D7IX-ray1.96A1-363[»]
4D7JX-ray1.55A1-363[»]
4LWAX-ray2.06A1-363[»]
4LWBX-ray2.15A1-363[»]
4UG5X-ray2.35A1-363[»]
4UG6X-ray1.81A1-363[»]
4UG7X-ray1.76A1-363[»]
4UG8X-ray1.89A1-363[»]
4UG9X-ray1.84A1-363[»]
4UGAX-ray1.90A1-363[»]
4UGBX-ray1.91A1-363[»]
4UGCX-ray1.80A1-363[»]
4UGDX-ray2.03A1-363[»]
4UGEX-ray2.14A1-363[»]
4UGFX-ray1.81A1-363[»]
4UGGX-ray2.36A1-363[»]
4UGHX-ray1.99A1-363[»]
4UGIX-ray1.80A1-363[»]
4UGJX-ray1.78A1-363[»]
4UGKX-ray1.62A1-363[»]
4UGLX-ray1.82A1-363[»]
4UGMX-ray2.09A1-363[»]
4UGNX-ray2.09A1-363[»]
4UGOX-ray2.38A1-363[»]
4UGPX-ray1.80A1-363[»]
4UGQX-ray1.85A1-363[»]
4UGRX-ray2.09A1-363[»]
4UGSX-ray1.99A1-363[»]
4UGTX-ray2.03A1-363[»]
4UGUX-ray1.80A1-363[»]
4UGVX-ray1.99A1-363[»]
4UGWX-ray1.90A1-363[»]
4UGXX-ray1.86A1-363[»]
4UGYX-ray1.80A1-363[»]
4UQRX-ray1.72A1-363[»]
4UQSX-ray2.15A1-363[»]
5G65X-ray2.03A1-363[»]
5G66X-ray1.76A1-363[»]
5G67X-ray1.97A1-363[»]
5G68X-ray1.63A1-363[»]
5G69X-ray2.02A1-363[»]
5G6AX-ray1.92A1-363[»]
5G6BX-ray1.80A1-363[»]
5G6CX-ray2.13A1-363[»]
5G6DX-ray1.82A1-363[»]
5G6EX-ray2.11A1-363[»]
5G6FX-ray2.26A1-363[»]
5G6GX-ray1.98A1-363[»]
5G6HX-ray1.91A1-363[»]
5G6IX-ray1.98A1-363[»]
5G6JX-ray1.88A1-363[»]
5G6KX-ray1.95A1-363[»]
5G6LX-ray2.03A1-363[»]
5G6MX-ray1.77A1-363[»]
5G6NX-ray1.91A1-363[»]
5G6OX-ray1.72A1-363[»]
5G6PX-ray2.18A1-363[»]
5G6QX-ray2.03A1-363[»]
ProteinModelPortaliO34453.
SMRiO34453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34453.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4362. LUCA.
HOGENOMiHOG000099920.
InParanoidiO34453.
KOiK00491.
OMAiWTWLIPP.
PhylomeDBiO34453.

Family and domain databases

Gene3Di3.90.340.10. 1 hit.
InterProiIPR017142. Nitric_oxide_synthase_Oase-su.
IPR004030. NOS_N.
[Graphical view]
PfamiPF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF037219. NOS_oxygenase. 1 hit.
SUPFAMiSSF56512. SSF56512. 1 hit.
PROSITEiPS60001. NOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKEILWNE AKAFIAACYQ ELGKEEEVKD RLADIKSEID LTGSYVHTKE
60 70 80 90 100
ELEHGAKMAW RNSNRCIGRL FWNSLNVIDR RDVRTKEEVR DALFHHIETA
110 120 130 140 150
TNNGKIRPTI TIFPPEEKGE KQVEIWNHQL IRYAGYESDG ERIGDPASCS
160 170 180 190 200
LTAACEELGW RGERTDFDLL PLIFRMKGDE QPVWYELPRS LVIEVPITHP
210 220 230 240 250
DIEAFSDLEL KWYGVPIISD MKLEVGGIHY NAAPFNGWYM GTEIGARNLA
260 270 280 290 300
DEKRYDKLKK VASVIGIAAD YNTDLWKDQA LVELNKAVLH SYKKQGVSIV
310 320 330 340 350
DHHTAASQFK RFEEQEEEAG RKLTGDWTWL IPPISPAATH IFHRSYDNSI
360
VKPNYFYQDK PYE
Length:363
Mass (Da):41,903
Last modified:May 26, 2009 - v2
Checksum:i4F889E68B4BDE5C6
GO

Sequence cautioni

The sequence BAA22306 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86417 Genomic DNA. Translation: BAA22306.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12592.2.
PIRiC69811.
RefSeqiNP_388644.2. NC_000964.3.
WP_003243309.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12592; CAB12592; BSU07630.
GeneIDi938802.
KEGGibsu:BSU07630.
PATRICi18973178. VBIBacSub10457_0803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86417 Genomic DNA. Translation: BAA22306.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12592.2.
PIRiC69811.
RefSeqiNP_388644.2. NC_000964.3.
WP_003243309.1. NZ_JNCM01000032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7VX-ray1.95A5-363[»]
1M7ZX-ray2.14A5-363[»]
2AMOX-ray2.60A/B30-363[»]
2AN0X-ray2.60A18-363[»]
2AN2X-ray2.60A18-363[»]
2FBZX-ray2.10X5-363[»]
2FC1X-ray2.00A5-363[»]
2FC2X-ray2.20A/B5-363[»]
4D3IX-ray2.09A1-363[»]
4D3JX-ray1.67A1-363[»]
4D3KX-ray2.02A/B1-363[»]
4D3MX-ray1.74A1-363[»]
4D3NX-ray2.13A1-363[»]
4D3OX-ray1.90A1-363[»]
4D3TX-ray1.55A1-363[»]
4D3UX-ray1.98A1-363[»]
4D3VX-ray1.88A1-363[»]
4D7HX-ray2.02A1-363[»]
4D7IX-ray1.96A1-363[»]
4D7JX-ray1.55A1-363[»]
4LWAX-ray2.06A1-363[»]
4LWBX-ray2.15A1-363[»]
4UG5X-ray2.35A1-363[»]
4UG6X-ray1.81A1-363[»]
4UG7X-ray1.76A1-363[»]
4UG8X-ray1.89A1-363[»]
4UG9X-ray1.84A1-363[»]
4UGAX-ray1.90A1-363[»]
4UGBX-ray1.91A1-363[»]
4UGCX-ray1.80A1-363[»]
4UGDX-ray2.03A1-363[»]
4UGEX-ray2.14A1-363[»]
4UGFX-ray1.81A1-363[»]
4UGGX-ray2.36A1-363[»]
4UGHX-ray1.99A1-363[»]
4UGIX-ray1.80A1-363[»]
4UGJX-ray1.78A1-363[»]
4UGKX-ray1.62A1-363[»]
4UGLX-ray1.82A1-363[»]
4UGMX-ray2.09A1-363[»]
4UGNX-ray2.09A1-363[»]
4UGOX-ray2.38A1-363[»]
4UGPX-ray1.80A1-363[»]
4UGQX-ray1.85A1-363[»]
4UGRX-ray2.09A1-363[»]
4UGSX-ray1.99A1-363[»]
4UGTX-ray2.03A1-363[»]
4UGUX-ray1.80A1-363[»]
4UGVX-ray1.99A1-363[»]
4UGWX-ray1.90A1-363[»]
4UGXX-ray1.86A1-363[»]
4UGYX-ray1.80A1-363[»]
4UQRX-ray1.72A1-363[»]
4UQSX-ray2.15A1-363[»]
5G65X-ray2.03A1-363[»]
5G66X-ray1.76A1-363[»]
5G67X-ray1.97A1-363[»]
5G68X-ray1.63A1-363[»]
5G69X-ray2.02A1-363[»]
5G6AX-ray1.92A1-363[»]
5G6BX-ray1.80A1-363[»]
5G6CX-ray2.13A1-363[»]
5G6DX-ray1.82A1-363[»]
5G6EX-ray2.11A1-363[»]
5G6FX-ray2.26A1-363[»]
5G6GX-ray1.98A1-363[»]
5G6HX-ray1.91A1-363[»]
5G6IX-ray1.98A1-363[»]
5G6JX-ray1.88A1-363[»]
5G6KX-ray1.95A1-363[»]
5G6LX-ray2.03A1-363[»]
5G6MX-ray1.77A1-363[»]
5G6NX-ray1.91A1-363[»]
5G6OX-ray1.72A1-363[»]
5G6PX-ray2.18A1-363[»]
5G6QX-ray2.03A1-363[»]
ProteinModelPortaliO34453.
SMRiO34453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004263.

Chemistry databases

BindingDBiO34453.

Proteomic databases

PaxDbiO34453.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12592; CAB12592; BSU07630.
GeneIDi938802.
KEGGibsu:BSU07630.
PATRICi18973178. VBIBacSub10457_0803.

Phylogenomic databases

eggNOGiCOG4362. LUCA.
HOGENOMiHOG000099920.
InParanoidiO34453.
KOiK00491.
OMAiWTWLIPP.
PhylomeDBiO34453.

Enzyme and pathway databases

BioCyciBSUB:BSU07630-MONOMER.
SABIO-RKO34453.

Miscellaneous databases

EvolutionaryTraceiO34453.

Family and domain databases

Gene3Di3.90.340.10. 1 hit.
InterProiIPR017142. Nitric_oxide_synthase_Oase-su.
IPR004030. NOS_N.
[Graphical view]
PfamiPF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF037219. NOS_oxygenase. 1 hit.
SUPFAMiSSF56512. SSF56512. 1 hit.
PROSITEiPS60001. NOS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNOSO_BACSU
AccessioniPrimary (citable) accession number: O34453
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: May 26, 2009
Last modified: November 30, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is similar to the oxygenase domain of eukaryotic nitric oxide synthases but lacks the reductase domain which, in eukaryotes, is responsible for transfer of electrons to the ferric heme during nitric oxide synthesis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.