[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-2. STRAIN=IFO 0734 / CBS 6917 / SIFF V-342a; DOI=10.1016/0022-2836(92)90236-D; PubMed=1404399 [NCBI, ExPASy, EBI, Israel, Japan] Iwaasa H., Takagi T., Shikama K.; "Amino acid sequence of yeast hemoglobin. A two-domain structure."; J. Mol. Biol. 227:948-954(1992).
[2]	SEQUENCE REVISION TO 389-390. Takagi T.; Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[3]	COFACTOR. PubMed=4798061 [NCBI, ExPASy, EBI, Israel, Japan] Oshino R., Asakura T., Takio K., Oshino N., Chance B., Hagihara B.; "Purification and molecular properties of yeast hemoglobin."; Eur. J. Biochem. 39:581-590(1973).
[4]	ABSORPTION SPECTROSCOPY, AND CIRCULAR DICHROISM ANALYSIS. DOI=10.1074/jbc.M206529200; PubMed=12192008 [NCBI, ExPASy, EBI, Israel, Japan] Kobayashi G., Nakamura T., Ohmachi H., Matsuoka A., Ochiai T., Shikama K.; "Yeast flavohemoglobin from Candida norvegensis. Its structural, spectral, and stability properties."; J. Biol. Chem. 277:42540-42548(2002).
[5]	REVIEW. DOI=10.1016/1357-2725(95)00084-3; PubMed=7584595 [NCBI, ExPASy, EBI, Israel, Japan] Shikama K., Matsuoka A., Iwaasa H.; "The unique structures of protozoan myoglobin and yeast hemoglobin: an evolutionary diversity."; Int. J. Biochem. Cell Biol. 27:1107-1115(1995).

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).
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.
COFACTOR: Binds 1 heme B group per subunit.
SUBCELLULAR LOCATION: Cytoplasm (By 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.
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

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Cross-references

Sequence databases

EMBL

X68849; CAA48729.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S26964; S26964.

3D structure databases

HSSP

P04252; 2VHB. [HSSP ENTRY / PDB]

ModBase

Q03331.

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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009636;	Biological process: response to toxin (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR000951; Ph_dOase_redase_FPNCR.
Graphical view of domain structure.

Pfam

PF00970; FAD_binding_6; 1.
PF00042; Globin; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00409; PHDIOXRDTASE.

PROSITE

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

ProtoNet

Q03331.

Other

UniRef

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

Keywords

Acetylation; Cytoplasm; Detoxification; Direct protein sequencing; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 390`	`389`	`Flavohemoprotein.`	`PRO_0000052459`
`DOMAIN`	`158 263`	`106`	`FAD-binding FR-type.`
`NP_BIND`	`214 217`	`4`	`FAD (By similarity).`
`NP_BIND`	`277 282`	`6`	`NADP (By similarity).`
`NP_BIND`	`382 385`	`4`	`FAD (By similarity).`
`REGION`	`10 151`	`142`	`Globin.`
`REGION`	`157 390`	`234`	`Reductase.`
`REGION`	`268 390`	`123`	`NAD or NADP-binding.`
`ACT_SITE`	`106 106`		`Charge relay system (By similarity).`
`ACT_SITE`	`148 148`		`Charge relay system (By similarity).`
`METAL`	`96 96`		`Iron (heme proximal ligand) (By similarity).`
`BINDING`	`196 196`		`FAD (By similarity).`
`SITE`	`40 40`	`1`	`Involved in heme-bound ligand stabilization and O-O bond activation (By similarity).`
`SITE`	`95 95`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`
`SITE`	`381 381`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine.`

Sequence information

Length: 390 AA [This is the length of the unprocessed precursor]

Molecular weight: 44363 Da [This is the MW of the unprocessed precursor]

CRC64: 8066E37384A15ED4 [This is a checksum on the sequence]

        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

Q03331 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