NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1128/JB.184.20.5714-5722.2002; PubMed=12270830 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki K., Ichimura A., Ogawa N., Hasebe A., Miyashita K.;
"Differential expression of two catechol 1,2-dioxygenases in Burkholderia sp. strain TH2.";
J. Bacteriol. 184:5714-5722(2002).

Comments

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

AB035325; BAC16771.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04252; 4VHB. [HSSP ENTRY / PDB]

ModBase

Q8GAZ4.

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.
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

PR00371; FPNCR.
PR00409; PHDIOXRDTASE.

PROSITE

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

Other

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

Keywords

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_0000052428`
`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`	`385 388`	`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`	`384 384`	`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: 43707 Da [This is the MW of the unprocessed precursor]

CRC64: D17DB36399BB717B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSAEHRAIV KATVPLLESG GEALTTHFYK TMLAEYPSVR PLFNQAHQQS GDQPRALANA 

        70         80         90        100        110        120 
VLMYARHIDQ LEQLGGLVSQ IVNKHVALNI LPEHYPIVGA CLLRAIREVL GAEIATDAVI 

       130        140        150        160        170        180 
EAWGAAYQQL ADLLIGLEEN VYVEKETATG GWRGTRAFVV ARKVKESDEI TSFYLRPADG 

       190        200        210        220        230        240 
GELLEFHPGQ YIGLKLIVDG EEIRRNYSLS AAANGREYRI SVKREPNGKA SNYLHDSVNE 

       250        260        270        280        290        300 
GATLDLLTPS GDFTLEHNDK PLVLISGGVG ITPTLAMLNA ALQTSRPIHF IHATRHGGVH 

       310        320        330        340        350        360 
AFRDHIDELA ARHPQLKRFY VYEKPRHDDE AHHAEGYIDE ARLIEWLPAT RDVDVYFLGP 

       370        380        390 
KSFMQAVKRH LKTIGVPEKQ SRYEFFGPAS ALD

Q8GAZ4 in FASTA format

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View entry in raw text format (no links)
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	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