NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RIMD 2210633 / Serotype O3:K6;
DOI=10.1016/S0140-6736(03)12659-1; PubMed=12620739 [NCBI, ExPASy, EBI, Israel, Japan]
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae.";
Lancet 361:743-749(2003).

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

U09005; AAA62190.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000031; BAC61072.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_799188.1; -.

3D structure databases

HSSP

P24232; 1GVH. [HSSP ENTRY / PDB]

ModBase

P40609.

Enzyme and pathway databases

BioCyc

VPAR223926:VP2809-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: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

P40609.

Genome annotation databases

1190359; -.

BA000031_GR; VP2809.

vpa:VP2809; -.

fig|223926.1.peg.2809; -.

Phylogenomic databases

HOGENOM

P40609; -.

Genome annotation databases

CMR

P40609; VP2809.

Other

ProtoNet

P40609.

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`	`1 394`	`394`	`Flavohemoprotein.`	`PRO_0000052450`
`DOMAIN`	`150 255`	`106`	`FAD-binding FR-type.`
`NP_BIND`	`204 207`	`4`	`FAD (By similarity).`
`NP_BIND`	`268 273`	`6`	`NADP (By similarity).`
`NP_BIND`	`387 390`	`4`	`FAD (By similarity).`
`REGION`	`1 136`	`136`	`Globin.`
`REGION`	`147 394`	`248`	`Reductase.`
`REGION`	`259 394`	`136`	`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`	`386 386`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`
`CONFLICT`	`118 118`		`D -> G (in Ref. 1; AAA62190).`

Sequence information

Length: 394 AA [This is the length of the unprocessed precursor]

Molecular weight: 44410 Da [This is the MW of the unprocessed precursor]

CRC64: 2B65A6A71C8AB7AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSNQTIEIV KATAPLIAET GPKLTAHFYD RMFTHNPELK DIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
ICAYAANIEN LPALLGAVEK IAHKHTSFLI TKDQYQIVGK HLIATIDELF NPGQEVLDAW 

       130        140        150        160        170        180 
AEAYGVLANV FIQREEQIYQ ANASQEGGWR GLREFELVGK QLESEHICSF VFKPTDGSKV 

       190        200        210        220        230        240 
TKYKPGQYLG IYINSDKFEN QEIRQYSLSS SVQENTYRIS VKREQGGKVS NYLHDELNIG 

       250        260        270        280        290        300 
DKVKLAAPAG DFFMDVDTNT PVVLISAGVG LTPTLSMLES LTEHHAPVTW VHATENSKHH 

       310        320        330        340        350        360 
AFKEHVNQLV TAKENMNALI WYNQPTAEDK IGEDFHFTGF VNLHEIEAAL KQDNVQVYFC 

       370        380        390 
GPVGFMQHVA KQLQELGVPQ EQFHYECFGP HKVV

P40609 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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