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Protein

Flavohemoprotein

Gene

SPAC869.02c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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).By similarity
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).By similarity

Catalytic activityi

2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • heme bBy similarityNote: Binds 1 heme b group per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Involved in heme-bound ligand stabilization and O-O bond activationBy similarity
Sitei113 – 1131Influences the redox potential of the prosthetic heme and FAD groupsBy similarity
Metal bindingi114 – 1141Iron (heme proximal ligand)PROSITE-ProRule annotationBy similarity
Active sitei124 – 1241Charge relay systemBy similarity
Active sitei167 – 1671Charge relay systemBy similarity
Binding sitei216 – 2161FADBy similarity
Sitei420 – 4201Influences the redox potential of the prosthetic heme and FAD groupsBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi232 – 2354FADBy similarity
Nucleotide bindingi301 – 3066NADPBy similarity
Nucleotide bindingi421 – 4244FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Detoxification

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD, NADP

Names & Taxonomyi

Protein namesi
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 namesi
ORF Names:SPAC869.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC869.02c.
PomBaseiSPAC869.02c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427FlavohemoproteinPRO_0000280219Add
BLAST

Proteomic databases

MaxQBiQ9URY5.

Interactioni

Protein-protein interaction databases

BioGridi278580. 9 interactions.
MINTiMINT-4707275.

Structurei

3D structure databases

ProteinModelPortaliQ9URY5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 285109FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 170143GlobinSequence analysisAdd
BLAST
Regioni176 – 427252ReductaseSequence analysisAdd
BLAST
Regioni290 – 427138NAD or NADP-bindingSequence analysisAdd
BLAST

Domaini

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.Curated

Sequence similaritiesi

Belongs to the globin family. Two-domain flavohemoproteins subfamily.PROSITE-ProRule annotation
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Sequence analysis
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000238921.
InParanoidiQ9URY5.
KOiK05916.
OMAiDQYQIVG.
OrthoDBiEOG73Z337.
PhylomeDBiQ9URY5.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF46458. SSF46458. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9URY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVEVNREN ADVANTNRQA NLAEGYEIKE LNESQKQYIR SSIPILESSG
60 70 80 90 100
VNLTKAFYQK MLGNYPEVLP YFNKAHQISL SQPRILAFAL LNYAKNIDDL
110 120 130 140 150
TSLSAFMDQI VVKHVGLQIK AEHYPIVGHC LLSTMQELLP SDVATPAFLE
160 170 180 190 200
AWTTAYGNLA KILIDSEKKV YQSQPWNGFV EFKVTELINE SSDVKSVYLG
210 220 230 240 250
PKDPAFRISH AHPGQYVSVL WEIPGLSHKT LREYSLSNRV DTCRNQFRIS
260 270 280 290 300
VRRVAGGVVS NFVHDNLKVG DIVGVSPPAG NFVYKRSEEN VNRPLLCFAG
310 320 330 340 350
GIGITPLIPI IETALLDGRK VNFCYSSRNY VSRPFKQWLE QLKLKYKENL
360 370 380 390 400
KLKEFFSEES SVTKEQIVDE VMTRIINEED LEKLDLSECD IYMLGPNNYM
410 420
RFVKQELVKL GVEPNKVQSE FFGPYIP
Length:427
Mass (Da):48,459
Last modified:May 1, 2000 - v1
Checksum:i869E5D4578F309D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB60012.1.
PIRiT39113.
RefSeqiNP_595017.1. NM_001020448.2.

Genome annotation databases

EnsemblFungiiSPAC869.02c.1; SPAC869.02c.1:pep; SPAC869.02c.
GeneIDi2542104.
KEGGispo:SPAC869.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB60012.1.
PIRiT39113.
RefSeqiNP_595017.1. NM_001020448.2.

3D structure databases

ProteinModelPortaliQ9URY5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278580. 9 interactions.
MINTiMINT-4707275.

Proteomic databases

MaxQBiQ9URY5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC869.02c.1; SPAC869.02c.1:pep; SPAC869.02c.
GeneIDi2542104.
KEGGispo:SPAC869.02c.

Organism-specific databases

EuPathDBiFungiDB:SPAC869.02c.
PomBaseiSPAC869.02c.

Phylogenomic databases

HOGENOMiHOG000238921.
InParanoidiQ9URY5.
KOiK05916.
OMAiDQYQIVG.
OrthoDBiEOG73Z337.
PhylomeDBiQ9URY5.

Miscellaneous databases

NextBioi20803176.
PROiQ9URY5.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF46458. SSF46458. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFHP_SCHPO
AccessioniPrimary (citable) accession number: Q9URY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 1, 2000
Last modified: December 9, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.