O34453 (NOSO_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nitric oxide synthase oxygenase
EC=1.14.13.165

Alternative name(s):
NOSoxy-like protein

Gene names

Name:	nos
Synonyms:	yflM
Ordered Locus Names:	BSU07630

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the production of nitric oxide. Ref.3
Catalytic activity	2 L-arginine + 3 NAD(P)H + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H2O. Ref.3
Cofactor	Heme group. Ref.3 Tetrahydrobiopterin (H4B). Can also use tetrahydrofolate (THF) in place of H4B but binds THF with much lower affinity than H4B. Ref.3
Subunit structure	Homodimer. Ref.3
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.
Sequence similarities	Belongs to the NOS family. Bacterial NOS oxygenase subfamily.
Sequence caution	The sequence BAA22306.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nitric oxide biosynthetic process Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	NADPH-hemoprotein reductase activity Inferred from Biological aspect of Ancestor. Source: RefGenome heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitric-oxide synthase activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 363

363

Nitric oxide synthase oxygenase

PRO_0000170953

Sites

Metal binding

66

1

Iron (heme axial ligand)

Secondary structure

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363

Helix Strand Turn

Details...

Helix

5 – 22

18

Helix

25 – 27

3

Helix

28 – 41

14

Helix

49 – 61

13

Helix

69 – 74

6

Beta strand

76 – 79

4

Helix

86 – 101

16

Helix

102 – 104

3

Beta strand

109 – 112

4

Beta strand

117 – 119

3

Beta strand

122 – 125

4

Beta strand

128 – 131

4

Beta strand

135 – 137

3

Turn

140 – 142

3

Helix

146 – 148

3

Helix

149 – 156

8

Turn

157 – 159

3

Beta strand

172 – 176

5

Beta strand

183 – 185

3

Turn

189 – 191

3

Beta strand

194 – 196

3

Helix

203 – 208

6

Beta strand

211 – 214

4

Beta strand

222 – 225

4

Beta strand

228 – 231

4

Helix

241 – 245

5

Turn

246 – 250

5

Turn

252 – 255

4

Helix

258 – 264

7

Helix

272 – 274

3

Helix

276 – 295

20

Helix

302 – 318

17

Helix

327 – 330

4

Beta strand

333 – 335

3

Helix

336 – 338

3

Helix

340 – 343

4

Beta strand

352 – 356

5

Sequences

	Sequence		Length	Mass (Da)
	O34453 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: 4F889E68B4BDE5C6	FASTA	363	41,903
	10 20 30 40 50 60 MEEKEILWNE AKAFIAACYQ ELGKEEEVKD RLADIKSEID LTGSYVHTKE ELEHGAKMAW 70 80 90 100 110 120 RNSNRCIGRL FWNSLNVIDR RDVRTKEEVR DALFHHIETA TNNGKIRPTI TIFPPEEKGE 130 140 150 160 170 180 KQVEIWNHQL IRYAGYESDG ERIGDPASCS LTAACEELGW RGERTDFDLL PLIFRMKGDE 190 200 210 220 230 240 QPVWYELPRS LVIEVPITHP DIEAFSDLEL KWYGVPIISD MKLEVGGIHY NAAPFNGWYM 250 260 270 280 290 300 GTEIGARNLA DEKRYDKLKK VASVIGIAAD YNTDLWKDQA LVELNKAVLH SYKKQGVSIV 310 320 330 340 350 360 DHHTAASQFK RFEEQEEEAG RKLTGDWTWL IPPISPAATH IFHRSYDNSI VKPNYFYQDK PYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86417 Genomic DNA. Translation: BAA22306.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12592.2.

PIR

C69811.

RefSeq

NP_388644.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M7V	X-ray	1.95	A	5-363	[»]
1M7Z	X-ray	2.14	A	5-363	[»]
2AMO	X-ray	2.60	A/B	6-363	[»]
2AN0	X-ray	2.60	A	6-363	[»]
2AN2	X-ray	2.60	A	6-363	[»]
2FBZ	X-ray	2.10	X	5-363	[»]
2FC1	X-ray	2.00	A	5-363	[»]
2FC2	X-ray	2.20	A/B	5-363	[»]

ProteinModelPortal

O34453.

SMR

O34453. Positions 5-363.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU07630.

Proteomic databases

PaxDb

O34453.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB12592; CAB12592; BSU07630.

GeneID

938802.

KEGG

bsu:BSU07630.

PATRIC

18973178. VBIBacSub10457_0803.

Organism-specific databases

GenoList

BSU07630. [Micado]

Phylogenomic databases

eggNOG

COG4362.

HOGENOM

HOG000099920.

KO

K00491.

ProtClustDB

CLSK872836.

Enzyme and pathway databases

BioCyc

BSUB:BSU07630-MONOMER.

Family and domain databases

Gene3D

3.90.340.10. 1 hit.

InterPro

IPR017142. Nitric_oxide_synthase_Oase-su.
IPR004030. NO_synthase_oxygenase_dom.
IPR026009. NOS.
[Graphical view]

PANTHER

PTHR19384:SF5. PTHR19384:SF5. 1 hit.

Pfam

PF02898. NO_synthase. 1 hit.
[Graphical view]

PIRSF

PIRSF037219. NOS_oxygenase. 1 hit.

SUPFAM

SSF56512. NO_synthase_oxygenase_reg. 1 hit.

PROSITE

PS60001. NOS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O34453.

Entry information

Entry name

NOSO_BACSU

Accession

Primary (citable) accession number: O34453

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program