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UniProtKB/Swiss-Prot entry Q8Z4M3

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information

Entry name

HMP_SALTI

Primary accession number

Q8Z4M3

Secondary accession number

Q7CBL4

Integrated into Swiss-Prot on

September 13, 2004

Sequence was last modified on

March 1, 2002 (Sequence version 1)

Annotations were last modified on

July 22, 2008 (Entry version 38)

Name and origin of the protein

Protein name

Flavohemoprotein

Synonyms

Hemoglobin-like protein
Flavohemoglobin
Nitric oxide dioxygenase
NO oxygenase
NOD
EC 1.14.12.17

Gene name

	Name:	hmp
	Synonyms:	hmpA
	OrderedLocusNames:	STY2803, t0300

From

Salmonella typhi

[TaxID: 601]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CT18;
DOI=10.1038/35101607; PubMed=11677608 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18.";
Nature 413:848-852(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700931 / Ty2;
DOI=10.1128/JB.185.7.2330-2337.2003; PubMed=12644504 [NCBI, ExPASy, EBI, Israel, Japan]
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18.";
J. Bacteriol. 185:2330-2337(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

AL627275; CAD02759.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014613; AAO68025.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_457086.1; -.
NP_804176.1; -.

3D structure databases

HSSP

P24232; 1GVH. [HSSP ENTRY / PDB]

SMR

Q8Z4M3; 1-396.

ModBase

Q8Z4M3.

Enzyme and pathway databases

BioCyc

SENT209261:T0300-MON; -.
SENT220341:STY2803-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

Q8Z4M3.

Genome annotation databases

GeneID

1067908; -.
1249112; -.

GenomeReviews

AL513382_GR; STY2803.
AE014613_GR; t0300.

KEGG

stt:t0300; -.
sty:STY2803; -.

Phylogenomic databases

HOGENOM

Q8Z4M3; -.

Genome annotation databases

CMR

Q8Z4M3; STY2803.

Other

ProtoNet

Q8Z4M3.

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_0000052446`
`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: 44031 Da [This is the MW of the unprocessed precursor]

CRC64: 388D57F8E9D1FC70 [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 NWLHHHANVG 

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

       310        320        330        340        350        360 
VHAFADEVSE LGRTLPRFTA HTWYREPTEA DRAQRVFDSE GLMDLSKLEA AISDPAMQFY 

       370        380        390 
LCGPVGFMQF AAKQLVSLGV NNENIHYECF GPHKVL

Q8Z4M3 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