NUCLEOTIDE SEQUENCE [MRNA].
Grabowski P.S., Laing K.J., Hardie L., Macguigan F., Ralston S., Secombes C.J.;
"Detection of mRNA for a nitric oxide synthase in macrophages and gill of rainbow trout challenged with an attenuated bacterial pathogen.";
(In) Moncada S., Stamler J., Gross S., Higgs E.A. (eds.); 4th International meeting on the biology of nitric oxide, Amelia Island, Florida, Sep. 1995, pp.10:48-48, Portland Press, Brookfield (1996).

Comments

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions.
CATALYTIC ACTIVITY: L-arginine + n NADPH + m O₂ = citrulline + nitric oxide + n NADP⁺.
COFACTOR: Heme group (By similarity).
COFACTOR: Binds 1 FAD (By similarity).
COFACTOR: Binds 1 FMN (By similarity).
COFACTOR: Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme (By similarity).
ENZYME REGULATION: Not stimulated by calcium/calmodulin (By similarity).
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X97013; CAA65736.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P29477; 1NOS. [HSSP ENTRY / PDB]

SMR

Q92091; 1-132.

ModBase

Q92091.

Ontologies

GO:0005516;	Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0004517;	Molecular function: nitric-oxide synthase activity (inferred from electronic annotation from InterPro).
GO:0006809;	Biological process: nitric oxide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR004030; NO_synthase_oxygenase_reg.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.

PROSITE

PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; PARTIAL.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q92091.

Phylogenomic databases

HOVERGEN

Q92091; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calmodulin-binding; FAD; FMN; Heme; Iron; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >470`	`>470`	`Nitric oxide synthase, inducible.`	`PRO_0000170939`
`DOMAIN`	`169 307`	`139`	`Flavodoxin-like.`
`NP_BIND`	`253 284`	`32`	`FMN (By similarity).`
`NP_BIND`	`398 409`	`12`	`FAD (By similarity).`
`REGION`	`139 159`	`21`	`Calmodulin-binding (Potential).`
`NON_TER`	`1 1`
`NON_TER`	`470 470`

Sequence information

Length: 470 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 53329 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 40B6717EE500B64D [This is a checksum on the sequence]

        10         20         30         40         50         60 
GWYMGTEIGV RDFCDYQRYN ILEEVGRRMG LETHKLSSLW KDQALVTINV AVTYSFQKNK 

        70         80         90        100        110        120 
VIITDHHSAA ESFMKHLETE FPPARRLPAD WDWLVPPMSG SLTPIFHQEM VNYILSPFFY 

       130        140        150        160        170        180 
YQPDPWMTHV WRNGEMCLKK QQISFKAVAR AALFSSTLMS RVLANRVRCT VLYATETGKS 

       190        200        210        220        230        240 
QTLAQRLNSM LNCAFNSRLL CMEDYNFSDM EQESLLVVVM STFGNGGSPG NGESFKKQLF 

       250        260        270        280        290        300 
SLQYLRNKSR YCVFGLGSRM YPQFCAFAHA VDAKLEELGA ERVTPTGEGD ELNGQEEAFS 

       310        320        330        340        350        360 
AWALTALKDA YKEFKIQGQL SLQLPGAERF CEAWDPLRHR VAVESCPQDR ITALSAIHSK 

       370        380        390        400        410        420 
AVLPMKLKSK HNLQSPQSSR STILVELERE RSPEVMDFAP GDHVGVFPGN LPQLVAGILK 

       430        440        450        460        470 
FLPQTPPTNQ CLRLGYRSDT FRVMRKTGRL LDASQHSLCL RHSPTSWTLP

Q92091 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools