NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC-B67;
DOI=10.1093/nar/gki297; PubMed=15781495 [NCBI, ExPASy, EBI, Israel, Japan]
Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.;
"The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen.";
Nucleic Acids Res. 33:1690-1698(2005).

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

AE017220; AAX66457.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_217538.1; -.

3D structure databases

SMR

Q57LF5; 1-396.

ModBase

Q57LF5.

Enzyme and pathway databases

BioCyc

SENT321314:SCH_2551-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

Q57LF5.

Genome annotation databases

GeneID

3335051; -.

GenomeReviews

AE017220_GR; SCH_2551.

KEGG

sec:SC2551; -.

NMPDR

fig|321314.4.peg.3146; -.

Phylogenomic databases

HOGENOM

Q57LF5; -.

Genome annotation databases

CMR

Q57LF5; SCH_2551.

Other

ProtoNet

Q57LF5.

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`	`1 396`	`396`	`Flavohemoprotein.`	`PRO_0000052444`
`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`	`389 392`	`4`	`FAD (By similarity).`
`REGION`	`1 136`	`136`	`Globin.`
`REGION`	`147 396`	`250`	`Reductase.`
`REGION`	`259 396`	`138`	`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`	`388 388`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`

Sequence information

Length: 396 AA [This is the length of the unprocessed precursor]

Molecular weight: 43932 Da [This is the MW of the unprocessed precursor]

CRC64: 0A4462748325ECFD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGT HLLATLDEMF NPGQEVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FIHREAEIYH ENASKDGGWE GTRPFRIVAK TPRSALITSF EFEPVDGGTV 

       190        200        210        220        230        240 
AEYRPGQYLG VWLKPEGFAH QEIRQYSLTR KPDGKGYRIA VKREDGGQVS NWLHHHASVG 

       250        260        270        280        290        300 
DVVHLAAPAG DFFMNVAADT PVSLISAGVG QTPMLAMLDT LAKGQHTAQV NWFHAAENGD 

       310        320        330        340        350        360 
VHAFADEVSE LGRTLPRFTA HTWYREPTEA DRAQRLFDSE GLMDVSKLEA AISDPAMQFY 

       370        380        390 
LCGPVGFMQF AAKQLVSLGV NNENIHYECF GPHKVL

Q57LF5 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