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Q9URY5 (FHP_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDetoxification
   Cellular componentCytoplasm
Nucleus
   LigandFAD
Flavoprotein
Heme
Iron
Metal-binding
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular detoxification of nitrogen compound

Inferred by curator. Source: GeneDB_Spombe

oxygen transport

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

mitochondrion

Inferred by curator. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

nitric oxide dioxygenase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

oxygen binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Flavohemoprotein
PRO_0000280219

Regions

Domain177 – 285109FAD-binding FR-type
Nucleotide binding232 – 2354FAD By similarity UniProtKB P24232
Nucleotide binding301 – 3066NADP By similarity UniProtKB Q03331
Nucleotide binding421 – 4244FAD By similarity UniProtKB P24232
Region28 – 170143Globin
Region176 – 427252Reductase
Region290 – 427138NAD or NADP-binding

Sites

Active site1241Charge relay system By similarity UniProtKB P24232
Active site1671Charge relay system By similarity UniProtKB P24232
Metal binding1141Iron (heme proximal ligand) By similarity
Binding site2161FAD By similarity UniProtKB P24232
Site581Involved in heme-bound ligand stabilization and O-O bond activation By similarity UniProtKB P24232
Site1131Influences the redox potential of the prosthetic heme and FAD groups By similarity UniProtKB P24232
Site4201Influences the redox potential of the prosthetic heme and FAD groups By similarity UniProtKB P24232

Sequences

Sequence LengthMass (Da)Tools
Q9URY5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 869E5D4578F309D6

FASTA42748,459
        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

« Hide

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. expand/collapse author list , 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: 972 / ATCC 24843.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB60012.1.
PIRT39113.
RefSeqNP_595017.1. NM_001020448.1.

3D structure databases

HSSPHSSP built from PDB template 4VHB based on UniProtKB P04252.
ProteinModelPortalQ9URY5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9URY5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC869.02c.1; SPAC869.02c.1:pep; SPAC869.02c.
GeneID2542104.
KEGGspo:SPAC869.02c.
NMPDRfig|4896.1.peg.4987.

Organism-specific databases

GeneDB_SpombeSPAC869.02c.

Phylogenomic databases

eggNOGfuNOG05360.
GeneTreeEFGT00050000001964.
HOGENOMHBG623097.
OMAYERLFEN.
OrthoDBEOG4C5GT7.

Gene expression databases

ArrayExpressQ9URY5.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR000971. Globin_subset.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:1.10.490.10. Globin_related. 1 hit.
KOK05916.
PfamPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
SUPFAMSSF46458. Globin_like. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFHP_SCHPO
AccessionPrimary (citable) accession number: Q9URY5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents