NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=AX3-1;
DOI=10.1247/csf.25.47; PubMed=10791894 [NCBI, ExPASy, EBI, Israel, Japan]
Iijima M., Shimizu H., Tanaka Y., Urushihara H.;
"Identification and characterization of two flavohemoglobin genes in Dictyostelium discoideum.";
Cell Struct. Funct. 25:47-55(2000).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(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 cell from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
FUNCTION: In the presence of oxygen and NADH, it has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2). Under anaerobic conditions, it also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity (By similarity).
CATALYTIC ACTIVITY: 2 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺.
COFACTOR: Binds 1 FAD per subunit (By similarity).
COFACTOR: Binds 1 heme B group per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
DEVELOPMENTAL STAGE: Accumulates in macrocysts.
INDUCTION: By submerged conditions, in growing cells.
DOMAIN: Consists of two distinct domains; a 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

AB025583; BAA83810.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AAFI02000190; EAL61168.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_629622.1; -.

3D structure databases

HSSP

P04252; 2VHB. [HSSP ENTRY / PDB]

ModBase

Q9UAG7.

Organism-specific databases

dictyBase

DDB0191099; fhbA.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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 EC).
GO:0019825;	Molecular function: oxygen binding (inferred from electronic annotation from InterPro).
GO:0005344;	Molecular function: oxygen transporter activity (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015671;	Biological process: oxygen transport (inferred from electronic annotation from InterPro).
GO:0009636;	Biological process: response to toxin (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
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

PR00406; CYTB5RDTASE.
PR00371; FPNCR.

PROSITE

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

ProtoNet

Q9UAG7.

Genome annotation databases

GeneID

3386245; -.

KEGG

ddi:DDB_0191099; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; 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`	`1 397`	`397`	`Flavohemoprotein A.`	`PRO_0000327849`
`DOMAIN`	`151 266`	`116`	`FAD-binding FR-type.`
`NP_BIND`	`208 211`	`4`	`FAD (By similarity).`
`NP_BIND`	`279 284`	`6`	`NADP (By similarity).`
`NP_BIND`	`390 393`	`4`	`FAD (By similarity).`
`REGION`	`1 141`	`141`	`Globin (By similarity).`
`REGION`	`150 397`	`248`	`Reductase (By similarity).`
`REGION`	`272 397`	`126`	`NAD or NADP-binding (By similarity).`
`ACT_SITE`	`94 94`		`Charge relay system (By similarity).`
`ACT_SITE`	`136 136`		`Charge relay system (By similarity).`
`METAL`	`84 84`		`Iron (heme proximal ligand) (By similarity).`
`BINDING`	`189 189`		`FAD (By similarity).`
`SITE`	`30 30`	`1`	`Involved in heme-bound ligand stabilization and O-O bond activation (By similarity).`
`SITE`	`83 83`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`
`SITE`	`389 389`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`

Sequence information

Length: 397 AA [This is the length of the unprocessed precursor]

Molecular weight: 43925 Da [This is the MW of the unprocessed precursor]

CRC64: 9641037821908183 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLSQQSISI IKATVPVLQV HGVNITTTFY RNMFKANPQL LNIFNHSNQR EGKQQNALAN 

        70         80         90        100        110        120 
TVLQAAIHID KLNELNLAPI VHKHVALGVL PEHYPIVGTN LLGAIKEVLQ DAATDEILGA 

       130        140        150        160        170        180 
WGEAYGVIAQ AFIDAEAALY KVTEEQIGGW RDTREFIVDR KVEESSNIIS FYFKPADGKP 

       190        200        210        220        230        240 
IATYIPGQYI TIKVPLTLEN GEQRTHIRHY SLSDTPSEQY YRISVKKEDA LKKSDPNGVV 

       250        260        270        280        290        300 
SNHLHANVKV GDKVLLSPPA GDYVVDQLSS NPILLVSGGV GITPLLSMAK ATLAKQPERE 

       310        320        330        340        350        360 
VTFVHSSKNK QYQPFANELS QLEKSNKVKV STVHSETDGQ ITKDKLEKFI NPSQIKDTKV 

       370        380        390 
FICGPVSFMS AINKQLIELG YPKENISYEI FGPLTNV

Q9UAG7 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