Reviewed, UniProtKB/Swiss-Prot Q03331 (FHP_CANNO)

Names and origin

Protein names	Recommended name:     Flavohemoprotein     EC=1.14.12.17 Alternative name(s):     Flavohemoglobin     Hemoglobin-like protein     Nitric oxide dioxygenase       Short name=NO oxygenase       Short name=NOD
Organism	Candida norvegensis (Yeast) (Candida mycoderma)
Taxonomic identifier	4921 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress By similarity. 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 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+).
Cofactor	Binds 1 FAD per subunit. Binds 1 heme B group per subunit.
Subcellular location	CytoplasmBy similarity.
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
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction 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-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 390	389	Flavohemoprotein		PRO_0000052459
Regions
	Domain	158 – 263	106	FAD-binding FR-type
	Nucleotide binding	214 – 217	4	FAD By similarity
	Nucleotide binding	277 – 282	6	NADP By similarity
	Nucleotide binding	382 – 385	4	FAD By similarity
	Region	10 – 151	142	Globin
	Region	157 – 390	234	Reductase
	Region	268 – 390	123	NAD or NADP-binding
Sites
	Active site	106	1	Charge relay system By similarity
	Active site	148	1	Charge relay system By similarity
	Metal binding	96	1	Iron (heme proximal ligand) By similarity
	Binding site	196	1	FAD By similarity
	Site	40	1	Involved in heme-bound ligand stabilization and O-O bond activation By similarity
	Site	95	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
	Site	381	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine

Sequences

	Sequence		Length	Mass (Da)
	Q03331-1 [UniParc]. Last modified May 29, 2007. Version 3. Checksum: 8066E37384A15ED4	FASTA	390	44,363
	10 20 30 40 50 60 MSAAKQLFKI VPLTPTEINF LQSLAPVVKE HGVTVTSTMY KYMFQTYPEV RSYFNMTNQK 70 80 90 100 110 120 TGRQPKVLAF SLYQYILHLN DLTPISGFVN QIVLKHCGLG IKPDQYPVVG ESLVQAFKMV 130 140 150 160 170 180 LGEAADEHFV EVFKKAYGNL AQTLIDAEAS VYKTLAWEEF KDFRVTKLVK EAEDVTSVYL 190 200 210 220 230 240 TPVDGFKLKP IIPGEYISFR WDIHNPDITD IQPREYSISQ DVKENEYRIS VRDIGIVSDY 250 260 270 280 290 300 INKKLQVGDI VPVHAPVGTM KYDSISKKGK VAVLAGGIGI TPMIPIIEHA LKDGKDVELY 310 320 330 340 350 360 YSNRSYQSEP FREFFSNLEK ENNGKFKLNN YISAENQKLQ VKDLEHINPD EYDVYLLGPV 370 380 390 AYMHEFKTYL VGKGVSDLKM EFFGPTDPDC

References

[1]	"Amino acid sequence of yeast hemoglobin. A two-domain structure." Iwaasa H., Takagi T., Shikama K. J. Mol. Biol. 227:948-954(1992) [PubMed: 1404399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2. Strain: IFO 0734 / CBS 6917 / SIFF V-342a.
[2]	Takagi T. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 389-390.
[3]	"Purification and molecular properties of yeast hemoglobin." Oshino R., Asakura T., Takio K., Oshino N., Chance B., Hagihara B. Eur. J. Biochem. 39:581-590(1973) [PubMed: 4798061] [Abstract] Cited for: COFACTOR.
[4]	"Yeast flavohemoglobin from Candida norvegensis. Its structural, spectral, and stability properties." Kobayashi G., Nakamura T., Ohmachi H., Matsuoka A., Ochiai T., Shikama K. J. Biol. Chem. 277:42540-42548(2002) [PubMed: 12192008] [Abstract] Cited for: ABSORPTION SPECTROSCOPY, CIRCULAR DICHROISM ANALYSIS.
[5]	"The unique structures of protozoan myoglobin and yeast hemoglobin: an evolutionary diversity." Shikama K., Matsuoka A., Iwaasa H. Int. J. Biochem. Cell Biol. 27:1107-1115(1995) [PubMed: 7584595] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X68849 mRNA. Translation: CAA48729.2.
PIR	S26964.
3D structure databases
HSSP	HSSP built from PDB template 2VHB based on UniProtKB P04252.
ModBase	Search...
Family and domain databases
InterPro	IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR000951. Ph_dOase_redase_FPNCR. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00409. PHDIOXRDTASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FHP_CANNO

Accession

Primary (citable) accession number: Q03331

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 29, 2007
Last modified:	November 25, 2008
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)