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

AE004091; AAG06052.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F83311; F83311.

RefSeq

NP_251354.1; -.

3D structure databases

HSSP

P04252; 1VHB. [HSSP ENTRY / PDB]

ModBase

Q9I0H4.

Enzyme and pathway databases

BioCyc

PAER208964:PA2664-MON; -.

Organism-specific databases

PseudoCAP

PA2664; -.

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:0015671;	Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01252; -; 1.
PBIL [Tree]

InterPro

IPR001709; FPN_cyt_redctse.
IPR012292; Globin.
IPR000971; Globin_subset.
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

PR00371; FPNCR.
PR00410; PHEHYDRXLASE.

PROSITE

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

BLOCKS

Q9I0H4.

Genome annotation databases

GeneID

882373; -.

GenomeReviews

AE004091_GR; PA2664.

KEGG

pae:PA2664; -.

Phylogenomic databases

HOGENOM

Q9I0H4; -.

Genome annotation databases

CMR

Q9I0H4; PA2664.

Other

ProtoNet

Q9I0H4.

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`	`1 393`	`393`	`Flavohemoprotein.`	`PRO_0000052439`
`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`	`150 393`	`244`	`Reductase.`
`REGION`	`260 393`	`134`	`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: 393 AA [This is the length of the unprocessed precursor]

Molecular weight: 43658 Da [This is the MW of the unprocessed precursor]

CRC64: 6384A119B51AD82B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSNAQRALI KATVPLLETG GEALITHFYR TMLGEYPEVR PLFNQAHQAS GDQPRALANG 

        70         80         90        100        110        120 
VLMYARHIDQ LQELGPLVAK VVNKHVSLQV LPEHYPIVGT CLLRAIREVL GEQIATDEVL 

       130        140        150        160        170        180 
EAWGAAYQQL ADLLIEAEES VYAASAQADG GWRGVRRFRV ARKQAESEEI TSFYLEPVDG 

       190        200        210        220        230        240 
QPLLAFQPGQ YIGLRLDIDG EEVRRNYSLS AASNGREYRI SVKREAGGRV SNYLHDRVAE 

       250        260        270        280        290        300 
GDELDLFPPA GDFVLRDSDK PLVLITAGVG ITPALAMLQE ALPQARPIRF IHCARHGGVH 

       310        320        330        340        350        360 
AFRDWIEDVS AQHEQVEHFF CYSEPRAGDS ADAEGLLSRE KLADWLPQER DLDAYFLGPR 

       370        380        390 
PFMAQVKRHL ADLGVPSQQC HYEFFGPAAA LDA

Q9I0H4 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