FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
CATALYTIC ACTIVITY: 2 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
COFACTOR: Binds 1 FAD per subunit (By similarity).
DOMAIN: Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins subfamily.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type 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

AE015451; AAN66433.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_742969.1; -.

3D structure databases

HSSP

P04252; 4VHB. [HSSP ENTRY / PDB]

ModBase

Q88PP0.

Enzyme and pathway databases

BioCyc

PPUT160488:PP_0808-MON; -.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0008941;	Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019825;	Molecular function: oxygen binding (inferred from electronic annotation from InterPro).
GO:0005344;	Molecular function: oxygen transporter activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015671;	Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
GO:0009636;	Biological process: response to toxin (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01252; -; 1.
PBIL [Tree]

InterPro

IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR000951; Ph_dOase_redase_FPNCR.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.490.10; Globin_related; 1.

Pfam

PF00970; FAD_binding_6; 1.
PF00042; Globin; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00409; PHDIOXRDTASE.

PROSITE

PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1044654; -.

GenomeReviews

AE015451_GR; PP_0808.

KEGG

ppu:PP_0808; -.

NMPDR

fig|160488.1.peg.799; -.

TIGR

PP_0808; -.

Phylogenomic databases

HOGENOM

Q88PP0; -.

Other

UniRef

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

Keywords

Complete proteome; Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 392`	`392`	`Flavohemoprotein.`	`PRO_0000052440`
`DOMAIN`	`153 256`	`104`	`FAD-binding FR-type.`
`NP_BIND`	`205 208`	`4`	`FAD (By similarity).`
`NP_BIND`	`268 273`	`6`	`NADP (By similarity).`
`NP_BIND`	`384 387`	`4`	`FAD (By similarity).`
`REGION`	`1 139`	`139`	`Globin.`
`REGION`	`150 392`	`243`	`Reductase.`
`REGION`	`260 392`	`133`	`NAD or NADP-binding.`
`ACT_SITE`	`95 95`		`Charge relay system (By similarity).`
`ACT_SITE`	`138 138`		`Charge relay system (By similarity).`
`METAL`	`85 85`		`Iron (heme proximal ligand) (By similarity).`
`BINDING`	`191 191`		`FAD (By similarity).`
`SITE`	`29 29`	`1`	`Involved in heme-bound ligand stabilization and O-O bond activation (By similarity).`
`SITE`	`84 84`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`
`SITE`	`383 383`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`

Sequence information

Length: 392 AA [This is the length of the unprocessed precursor]

Molecular weight: 43127 Da [This is the MW of the unprocessed precursor]

CRC64: 81BE6B3D092EDA7C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLNAEQRAII KATVPLLESG GEALTTHFYK MMLSEYPEVR PLFNQAHQAS GDQPRALANG 

        70         80         90        100        110        120 
VLMYARHIDQ LEQLGGLVGQ IINKHVALQI LPEHYPIVGS CLLRAIEEVL GKDIATPAVI 

       130        140        150        160        170        180 
DAWGAAYGQL ADILIGAEEN LYKEKEEAEG GWRGTREFRL VRREQESSEI VSFYFAPVDG 

       190        200        210        220        230        240 
MPVLKAEPGQ YIGLKLDIDG AEQRRNYSLS ALCDGKEYRI SVKREAGGKV SNYLHDELKV 

       250        260        270        280        290        300 
GDTLQLFPPA GDFTLAASDK PLVLISGGVG ITPTLAMLQA ALQTRREVHF IHCARNGAVH 

       310        320        330        340        350        360 
AFRDWIDGLA ARHPQLKRFY CYAEPEGGAA ADAVGLLSED LLAEWLPQER DVDAYFLGPK 

       370        380        390 
GFMAAVKRQL KGLGVPEQQS RYEFFGPAAA LE

Q88PP0 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