Reviewed, UniProtKB/Swiss-Prot Q9URY5 (FHP_SCHPO)

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

Gene names

ORF Names:

SPAC869.02c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	427 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 fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress By similarity. UniProtKB P39676 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. UniProtKB P39676
Catalytic activity	2 NO + 2 O2 + NAD(P)H = 2 NO3- + NAD(P)+. UniProtKB P39676
Cofactor	Binds 1 FAD per subunit By similarity. UniProtKB Q03331 Binds 1 heme B group per subunit By similarity. UniProtKB Q03331
Subcellular location	Cytoplasm. Nucleus. Ref.2
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 Nucleus
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	detoxification of nitrogen compound Inferred by curator. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe mitochondrion Inferred by curator. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	Flavohemoprotein		PRO_0000280219
Regions
	Domain	177 – 285	109	FAD-binding FR-type
	Nucleotide binding	232 – 235	4	FAD By similarity UniProtKB P24232
	Nucleotide binding	301 – 306	6	NADP By similarity UniProtKB Q03331
	Nucleotide binding	421 – 424	4	FAD By similarity UniProtKB P24232
	Region	28 – 170	143	Globin
	Region	176 – 427	252	Reductase
	Region	290 – 427	138	NAD or NADP-binding
Sites
	Active site	124	1	Charge relay system By similarity UniProtKB P24232
	Active site	167	1	Charge relay system By similarity UniProtKB P24232
	Metal binding	114	1	Iron (heme proximal ligand) By similarity
	Binding site	216	1	FAD By similarity UniProtKB P24232
	Site	58	1	Involved in heme-bound ligand stabilization and O-O bond activation By similarity UniProtKB P24232
	Site	113	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity UniProtKB P24232
	Site	420	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity UniProtKB P24232

Sequences

	Sequence		Length	Mass (Da)
	Q9URY5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 869E5D4578F309D6	FASTA	427	48,459
	10 20 30 40 50 60 MSSVEVNREN ADVANTNRQA NLAEGYEIKE LNESQKQYIR SSIPILESSG VNLTKAFYQK 70 80 90 100 110 120 MLGNYPEVLP YFNKAHQISL SQPRILAFAL LNYAKNIDDL TSLSAFMDQI VVKHVGLQIK 130 140 150 160 170 180 AEHYPIVGHC LLSTMQELLP SDVATPAFLE AWTTAYGNLA KILIDSEKKV YQSQPWNGFV 190 200 210 220 230 240 EFKVTELINE SSDVKSVYLG PKDPAFRISH AHPGQYVSVL WEIPGLSHKT LREYSLSNRV 250 260 270 280 290 300 DTCRNQFRIS VRRVAGGVVS NFVHDNLKVG DIVGVSPPAG NFVYKRSEEN VNRPLLCFAG 310 320 330 340 350 360 GIGITPLIPI IETALLDGRK VNFCYSSRNY VSRPFKQWLE QLKLKYKENL KLKEFFSEES 370 380 390 400 410 420 SVTKEQIVDE VMTRIINEED LEKLDLSECD IYMLGPNNYM RFVKQELVKL GVEPNKVQSE FFGPYIP

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB60012.1.
PIR	T39113.
RefSeq	NP_595017.1.
3D structure databases
HSSP	HSSP built from PDB template 4VHB based on UniProtKB P04252.
ModBase	Search...
Genome annotation databases
GeneID	2542104.
KEGG	spo:SPAC869.02c.
NMPDR	fig|4896.1.peg.4987.
Organism-specific databases
GeneDB_Spombe	SPAC869.02c.
Phylogenomic databases
OMA	Q9URY5. FNMAHQE.
Enzyme and pathway databases
BRENDA	1.14.12.17. 653.
Gene expression databases
ArrayExpress	Q9URY5.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. 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]
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FHP_SCHPO

Accession

Primary (citable) accession number: Q9URY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)