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

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Cross-references

Sequence databases

EMBL

BX640417; CAE42489.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_880857.1; -.

3D structure databases

ModBase

Q7TTP0.

Enzyme and pathway databases

BioCyc

BPER257313:BP2212-MON; -.

Ontologies

GO:0008941;	Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
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.
IPR001032; Leghaemoglobin.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
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

PR00410; PHEHYDRXLASE.
PR00188; PLANTGLOBIN.

PROSITE

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

Genome annotation databases

2666010; -.

BX470248_GR; BP2212.

bpe:BP2212; -.

fig|257313.1.peg.1931; -.

Phylogenomic databases

HOGENOM

Q7TTP0; -.

Genome annotation databases

CMR

Q7TTP0; BP2212.

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`	`1 402`	`402`	`Flavohemoprotein.`	`PRO_0000052427`
`DOMAIN`	`152 261`	`110`	`FAD-binding FR-type.`
`NP_BIND`	`206 209`	`4`	`FAD (By similarity).`
`NP_BIND`	`274 279`	`6`	`NADP (By similarity).`
`NP_BIND`	`395 398`	`4`	`FAD (By similarity).`
`REGION`	`1 138`	`138`	`Globin.`
`REGION`	`149 402`	`254`	`Reductase.`
`REGION`	`265 402`	`138`	`NAD or NADP-binding.`
`ACT_SITE`	`95 95`		`Charge relay system (By similarity).`
`ACT_SITE`	`137 137`		`Charge relay system (By similarity).`
`METAL`	`85 85`		`Iron (heme proximal ligand) (By similarity).`
`BINDING`	`190 190`		`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`	`394 394`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`

Sequence information

Length: 402 AA [This is the length of the unprocessed precursor]

Molecular weight: 43754 Da [This is the MW of the unprocessed precursor]

CRC64: 5720B2A5F54CEF63 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSPEVRALV KATAPVLKEH GEALTRHFYT RMLGGNPELR QLFNQGHQQS GQQQQALAAA 

        70         80         90        100        110        120 
VAAYAEHIDD PSVLLQVVER IAHKHVSLGV RAEHYAIVGK HLLASIREVL GEAATDELID 

       130        140        150        160        170        180 
AWAAAYGQLA DLLIGRERAL YAAAASRDGG WTGWRAFKVV RKTPESAEIT SFYLAPADGG 

       190        200        210        220        230        240 
ATPDYLPGQY VSVRVYVPEL GLMQPRQYSL SEAPGMPGQL RISVKREAGS PAGMVSGTLH 

       250        260        270        280        290        300 
NRINEGDVLD VSPPQGDFTL DAEDGRPVVL LSGGVGLTPM VSMLNHLTAR DDGRQIRFVH 

       310        320        330        340        350        360 
ACREAGVHAM KEHINALAAK RPNVRKAVFY ERVGADDRRG VDYDYEGRVD LHAIRDEVIL 

       370        380        390        400 
PDADYYLCGP LPFMQAQRRA LADLGVAEHR IHAEVFGTGG VA

Q7TTP0 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