[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN RESISTANCE TO NITRIC OXIDE. STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023; DOI=10.1074/jbc.273.20.12543; PubMed=9575213 [NCBI, ExPASy, EBI, Israel, Japan] Crawford M.J., Goldberg D.E.; "Role for the Salmonella flavohemoglobin in protection from nitric oxide."; J. Biol. Chem. 273:12543-12547(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=LT2 / SGSC1412 / ATCC 700720; DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan] McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.; "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; Nature 413:852-856(2001).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. STRAIN=LT2; PubMed=2134182 [NCBI, ExPASy, EBI, Israel, Japan] Steiert J.G., Urbanowski M.L., Stauffer L.T., Plamann M.D., Stauffer G.V.; "Nucleotide sequence of the Salmonella typhimurium glyA gene."; DNA Seq. 1:107-113(1990).
[4]	INDUCTION. DOI=10.1074/jbc.273.51.34028; PubMed=9852058 [NCBI, ExPASy, EBI, Israel, Japan] Crawford M.J., Goldberg D.E.; "Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide."; J. Biol. Chem. 273:34028-34032(1998).
[5]	ROLE IN NITRIC OXIDE DETOXIFICATION. DOI=10.1128/IAI.70.8.4399-4405.2002; PubMed=12117950 [NCBI, ExPASy, EBI, Israel, Japan] Stevanin T.M., Poole R.K., Demoncheaux E.A.G., Read R.C.; "Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages."; Infect. Immun. 70:4399-4405(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.
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).
SUBUNIT: Monomer.
INDUCTION: By nitric oxide.
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

AF020388; AAC24484.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008816; AAL21450.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15816; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

A48427; A48427.

RefSeq

NP_461491.1; -.

3D structure databases

HSSP

P24232; 1GVH. [HSSP ENTRY / PDB]

SMR

P26353; 1-396.

ModBase

P26353.

Enzyme and pathway databases

BioCyc

STYP99287:STM2556-MON; -.

Organism-specific databases

StyGene

SG10170; hmp.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0008941;	Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019825;	Molecular function: oxygen binding (inferred from electronic annotation from InterPro).
GO:0005344;	Molecular function: oxygen transporter activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015671;	Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
GO:0009636;	Biological process: response to toxin (inferred from electronic annotation from UniProtKB-KW).
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).

ProtoNet

P26353.

Genome annotation databases

GeneID

1254078; -.

GenomeReviews

AE006468_GR; STM2556.

KEGG

stm:STM2556; -.

NMPDR

fig|99287.1.peg.2470; -.

Phylogenomic databases

HOGENOM

P26353; -.

Genome annotation databases

CMR

P26353; STM2556.

Other

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_0000052447`
`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`	`1 138`	`138`	`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).`
`CONFLICT`	`202 203`		`EI -> VF (in Ref. 1; AAC24484).`
`CONFLICT`	`242 242`		`G -> V (in Ref. 1; AAC24484).`
`CONFLICT`	`330 330`		`S -> A (in Ref. 1; AAC24484).`

Sequence information

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

Molecular weight: 43992 Da [This is the MW of the unprocessed precursor]

CRC64: 90D0FBCB239C87C5 [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 
DGVHLAAPAG DFFMNVAADT PVSLISAGVG QTPMLAMLDT LAKEQHTAQV NWFHAAENGD 

       310        320        330        340        350        360 
VHAFADEVSE LGRTLPRFTA HTWYREPTES DRAQRLFDSE GLMDLSKLEA AISDPAMQFY 

       370        380        390 
LCGPVGFMQF AAKQLVSLGV NNENIHYECF GPHKVL

P26353 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