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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Iron (heme axial ligand)

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Nitric oxide synthase oxygenasePRO_0000170953Add
BLAST

Proteomic databases

PaxDbiO34453.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004263.

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2119Combined sources
Helixi25 – 273Combined sources
Helixi28 – 4215Combined sources
Helixi49 – 6113Combined sources
Helixi69 – 746Combined sources
Beta strandi76 – 794Combined sources
Helixi86 – 10116Combined sources
Helixi102 – 1043Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi141 – 1444Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 1579Combined sources
Beta strandi172 – 1765Combined sources
Beta strandi183 – 1853Combined sources
Helixi189 – 1913Combined sources
Beta strandi194 – 1963Combined sources
Helixi203 – 2086Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi228 – 2314Combined sources
Helixi241 – 2455Combined sources
Turni246 – 2505Combined sources
Turni252 – 2554Combined sources
Helixi258 – 2647Combined sources
Helixi272 – 2743Combined sources
Helixi276 – 29520Combined sources
Helixi302 – 31918Combined sources
Helixi327 – 3304Combined sources
Beta strandi333 – 3353Combined sources
Helixi336 – 3383Combined sources
Helixi340 – 3434Combined sources
Beta strandi352 – 3565Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO34453.
SMRiO34453. Positions 5-363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34453.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4362. LUCA.
HOGENOMiHOG000099920.
InParanoidiO34453.
KOiK00491.
OMAiWTWLIPP.
OrthoDBiEOG6B09QB.
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 BAA22306.1 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
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[»]
ProteinModelPortaliO34453.
SMRiO34453. Positions 5-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004263.

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.
OrthoDBiEOG6B09QB.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of the Bacillus subtilis genome reveal genes for a new two-component system, three spore germination proteins, an iron uptake system and a general stress response protein."
    Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.
    Gene 194:191-199(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / AC327.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis."
    Adak S., Aulak K.S., Stuehr D.J.
    J. Biol. Chem. 277:16167-16171(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
  4. "Structure of a nitric oxide synthase heme protein from Bacillus subtilis."
    Pant K., Bilwes A.M., Adak S., Stuehr D.J., Crane B.R.
    Biochemistry 41:11071-11079(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

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: February 17, 2016
This is version 128 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.