Q54D73 (FHBB_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Flavohemoprotein B
EC=1.14.12.17

Alternative name(s):
DdFHb
Flavohemoglobin B
Hemoglobin-like protein B
Nitric oxide dioxygenase B
Short name=NO oxygenase B
Short name=NOD B

Gene names

Name:	fhbB
ORF Names:	DDB_G0292380

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.1
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 Reference proteome
Gene Ontology (GO)
Biological process	response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phagocytic vesicle Inferred from direct assay Ref.3. Source: dictyBase
Molecular function	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 – 423	423	Flavohemoprotein B		PRO_0000327850
Regions
	Domain	150 – 268	119	FAD-binding FR-type
	Nucleotide binding	212 – 215	4	FAD By similarity
	Nucleotide binding	281 – 286	6	NADP By similarity
	Nucleotide binding	400 – 403	4	FAD By similarity
	Region	1 – 140	140	Globin
	Region	149 – 423	275	Reductase By similarity
	Region	274 – 423	150	NAD or NADP-binding By similarity
Sites
	Active site	93	1	Charge relay system By similarity
	Active site	135	1	Charge relay system By similarity
	Metal binding	83	1	Iron (heme proximal ligand) By similarity
	Binding site	188	1	FAD By similarity
	Site	29	1	Involved in heme-bound ligand stabilization and O-O bond activation By similarity
	Site	82	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
	Site	399	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
Experimental info
	Sequence conflict	366	1	A → D in BAA83811. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54D73 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 3768C17E89D6D70C	FASTA	423	48,206
	10 20 30 40 50 60 MLSQKSIQII KSTVPLLEKY GVEITSLFYK NMFEAQPQFL NIFNHSNQRN QKQPVALANT 70 80 90 100 110 120 ILQSAIHIEK LNEINLMPIV HKHVALGITP EMYPIVGAHL LGAMKTVMQD EATPEIMAAW 130 140 150 160 170 180 TEAYRAVAQA FMDAEEDLYF ETEEQIGGWK DTREFVVDRI EEETPLIKSF YFKAYDGKEI 190 200 210 220 230 240 ATYIPGQYIT VKITLPGDGV DVPTDKMRTY VRHYSLSDKP NDEYYRISIK KELGKNTPNG 250 260 270 280 290 300 IVSNHFHNNI KVGDVVPMSV PAGDFVVNND SETPILLICG GVGINPLFSM LKETLVQQPD 310 320 330 340 350 360 RKINFIFSTH CESSQPFKEE LKQLEDDYKE TGNLKINLVY SENQGHINKE IIEKYSTQHV 370 380 390 400 410 420 DQAEIAETDV YICGPVPFMM QVNKDLLQLG FHKENVHYEL FGPLTPVLEE NQMLRGVKNI IEN

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.
[3]	"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed: 16926386] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: AX2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB025584 mRNA. Translation: BAA83811.1. AAFI02000190 Genomic DNA. Translation: EAL61169.1.
RefSeq	XP_629623.1. XM_629621.1.
3D structure databases
HSSP	HSSP built from PDB template 4VHB based on UniProtKB P04252.
ProteinModelPortal	Q54D73.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191088; DDB0191088; DDB_G0292380.
GeneID	8628686.
GenomeReviews	Gene locus fhbB in contig CM000155_GR.
KEGG	ddi:DDB_G0292380.
Organism-specific databases
dictyBase	DDB_G0292380. fhbB.
Phylogenomic databases
eggNOG	KOG3378.
GeneTree	EPrGT00050000005075.
HOGENOM	HBG623097.
OMA	STHCESS.
PhylomeDB	Q54D73.
ProtClustDB	CLSZ2429408.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR009050. Globin-like. IPR012292. Globin_dom. IPR000971. Globin_subset. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
KO	K05916.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
SUPFAM	SSF46458. Globin_like. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FHBB_DICDI

Accession

Primary (citable) accession number: Q54D73
Secondary accession number(s): Q9UAG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)