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

AE017194; AAS40500.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_977892.1; -.

3D structure databases

ModBase

Q73B49.

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

IPR012292; Globin.
IPR013316; Globin_annelid-type.
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

PR00410; PHEHYDRXLASE.
PR01907; WORMGLOBIN.

PROSITE

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

BLOCKS

Q73B49.

Genome annotation databases

GeneID

2749014; -.

GenomeReviews

AE017194_GR; BCE_1571.

KEGG

bca:BCE_1571; -.

NMPDR

fig|222523.1.peg.1564; -.

TIGR

BCE_1571; -.

Phylogenomic databases

HOGENOM

Q73B49; -.

Other

ProtoNet

Q73B49.

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_0000052420`
`DOMAIN`	`150 260`	`111`	`FAD-binding FR-type.`
`NP_BIND`	`204 207`	`4`	`FAD (By similarity).`
`NP_BIND`	`273 278`	`6`	`NADP (By similarity).`
`NP_BIND`	`394 397`	`4`	`FAD (By similarity).`
`REGION`	`1 136`	`136`	`Globin.`
`REGION`	`147 402`	`256`	`Reductase.`
`REGION`	`264 402`	`139`	`NAD or NADP-binding.`
`ACT_SITE`	`95 95`		`Charge relay system (By similarity).`
`ACT_SITE`	`135 135`		`Charge relay system (By similarity).`
`METAL`	`85 85`		`Iron (heme proximal ligand) (By similarity).`
`BINDING`	`188 188`		`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`	`393 393`	`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: 44954 Da [This is the MW of the unprocessed precursor]

CRC64: B7CC601EC87E3192 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSEKTIEIV KSTVPLLQEK GVEITTRFYE ILFSEHPELL NIFNHTNQKK GRQQQALANA 

        70         80         90        100        110        120 
VYAAATYIDN LEVIIPVVKQ IGHKHRSLGI KAEHYPIVGT CLLRAIKEVA GAPDEVLNAW 

       130        140        150        160        170        180 
GEAYGVIADA FISIEAEMYE EAAHKEGGWK DFRNFVVVKK VKESDVITSF YLKPEDGGKV 

       190        200        210        220        230        240 
SSFIPGQYVT VQINIEGETY THNRQYSLSD APGKEYYRIS VKKEKGVDTP DGKVSNYLHD 

       250        260        270        280        290        300 
HVKEGDMLPV SAPAGDFVLN MDSTLPVVLI SGGVGITPMM SMLNTLIEQD SKRNVCFVHA 

       310        320        330        340        350        360 
ALNSNTHAMK EHVEALDNEY EQVKAYTCYS APTEKDLEMK NFDKEGLIEA EWLQTIIPTT 

       370        380        390        400 
EAEFYFCGPV AFMKHINATL TDLGVKQEHI HYEFFGPAAS LQ

Q73B49 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