Reviewed, UniProtKB/Swiss-Prot Q9UAG7 (FHBA_DICDI)

Names and origin

Protein names

Recommended name:
    Flavohemoprotein A
    EC=1.14.12.17
Alternative name(s):
    Flavohemoglobin A
    DdFHa
    Hemoglobin-like protein A
    Nitric oxide dioxygenase A
      Short name=NO oxygenase A
      Short name=NOD A

Gene names

Name:	fhbA
ORF Names:	DDB_G0292378

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 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. Ref.1 In the presence of oxygen and NADH, it has NADH oxidase activity, which leads to the generation of superoxide and H2O2. 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. Binds 1 heme B group per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Developmental stage	Accumulates in macrocysts. Ref.1
Induction	By submerged conditions, in growing cells. Ref.1
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.
Sequence similarities	Belongs to the globin family. Two-domain flavohemoproteins subfamily. In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Detoxification Oxygen transport Transport
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: UniProtKB-KW response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: EC oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 397	397	Flavohemoprotein A		PRO_0000327849
Regions
	Domain	151 – 266	116	FAD-binding FR-type
	Nucleotide binding	208 – 211	4	FAD By similarity
	Nucleotide binding	279 – 284	6	NADP By similarity
	Nucleotide binding	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
Sites
	Active site	94	1	Charge relay system By similarity
	Active site	136	1	Charge relay system By similarity
	Metal binding	84	1	Iron (heme proximal ligand) By similarity
	Binding site	189	1	FAD By similarity
	Site	30	1	Involved in heme-bound ligand stabilization and O-O bond activation By similarity
	Site	83	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
	Site	389	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UAG7-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 9641037821908183	FASTA	397	43,925
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of two flavohemoglobin genes in Dictyostelium discoideum." Iijima M., Shimizu H., Tanaka Y., Urushihara H. Cell Struct. Funct. 25:47-55(2000) [PubMed: 10791894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, INDUCTION. Strain: AX3-1.
[2]	"The genome of the social amoeba Dictyostelium discoideum." 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. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB025583 mRNA. Translation: BAA83810.1. AAFI02000190 Genomic DNA. Translation: EAL61168.1.
RefSeq	XP_629622.1.
3D structure databases
HSSP	HSSP built from PDB template 2VHB based on UniProtKB P04252.
ModBase	Search...
Genome annotation databases
GeneID	3386245.
KEGG	ddi:DDB_0191099.
Organism-specific databases
dictyBase	DDB_G0292378. fhbA.
Phylogenomic databases
OMA	Q9UAG7. FNMAHQE.
Enzyme and pathway databases
BRENDA	1.14.12.17. 424.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012292. Globin. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FHBA_DICDI

Accession

Primary (citable) accession number: Q9UAG7
Secondary accession number(s): Q54D74

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)