FHP_SCHPO
ID FHP_SCHPO Reviewed; 427 AA.
AC Q9URY5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Flavohemoprotein;
DE EC=1.14.12.17;
DE AltName: Full=Flavohemoglobin;
DE AltName: Full=Hemoglobin-like protein;
DE AltName: Full=Nitric oxide dioxygenase;
DE Short=NO oxygenase;
DE Short=NOD;
GN ORFNames=SPAC869.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB60012.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Is involved in NO detoxification in an aerobic process,
CC termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and
CC NAD(P)H to convert NO to nitrate, which protects the fungus from
CC various noxious nitrogen compounds. Therefore, plays a central role in
CC the inducible response to nitrosative stress (By similarity).
CC {ECO:0000250|UniProtKB:P39676}.
CC -!- FUNCTION: In the presence of oxygen and NADH, it has NADH oxidase
CC activity, which leads to the generation of superoxide and H(2)O(2).
CC Under anaerobic conditions, it also exhibits nitric oxide reductase and
CC FAD reductase activities. However, all these reactions are much lower
CC than NOD activity (By similarity). {ECO:0000250|UniProtKB:P39676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.12.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.17;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q03331};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q03331};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q03331};
CC Note=Binds 1 heme b group per subunit. {ECO:0000250|UniProtKB:Q03331};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: Consists of two distinct domains; a N-terminal heme-containing
CC oxygen-binding domain and a C-terminal reductase domain with binding
CC sites for FAD and NAD(P)H. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00238}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255}.
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DR EMBL; CU329670; CAB60012.1; -; Genomic_DNA.
DR PIR; T39113; T39113.
DR RefSeq; NP_595017.1; NM_001020448.2.
DR AlphaFoldDB; Q9URY5; -.
DR SMR; Q9URY5; -.
DR BioGRID; 278580; 9.
DR STRING; 4896.SPAC869.02c.1; -.
DR MaxQB; Q9URY5; -.
DR PaxDb; Q9URY5; -.
DR PRIDE; Q9URY5; -.
DR EnsemblFungi; SPAC869.02c.1; SPAC869.02c.1:pep; SPAC869.02c.
DR GeneID; 2542104; -.
DR KEGG; spo:SPAC869.02c; -.
DR PomBase; SPAC869.02c; -.
DR VEuPathDB; FungiDB:SPAC869.02c; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_12_0_1; -.
DR InParanoid; Q9URY5; -.
DR OMA; EENHTEF; -.
DR PhylomeDB; Q9URY5; -.
DR PRO; PR:Q9URY5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IC:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; ISS:PomBase.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IGI:PomBase.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IGI:PomBase.
DR GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR023950; Hmp.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW NAD; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..427
FT /note="Flavohemoprotein"
FT /id="PRO_0000280219"
FT DOMAIN 177..285
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 28..170
FT /note="Globin"
FT /evidence="ECO:0000255"
FT REGION 176..427
FT /note="Reductase"
FT /evidence="ECO:0000255"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT BINDING 114
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250|UniProtKB:P24232,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT BINDING 232..235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT BINDING 301..306
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 421..424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT SITE 58
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT SITE 113
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250|UniProtKB:P24232"
FT SITE 420
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250|UniProtKB:P24232"
SQ SEQUENCE 427 AA; 48459 MW; 869E5D4578F309D6 CRC64;
MSSVEVNREN ADVANTNRQA NLAEGYEIKE LNESQKQYIR SSIPILESSG VNLTKAFYQK
MLGNYPEVLP YFNKAHQISL SQPRILAFAL LNYAKNIDDL TSLSAFMDQI VVKHVGLQIK
AEHYPIVGHC LLSTMQELLP SDVATPAFLE AWTTAYGNLA KILIDSEKKV YQSQPWNGFV
EFKVTELINE SSDVKSVYLG PKDPAFRISH AHPGQYVSVL WEIPGLSHKT LREYSLSNRV
DTCRNQFRIS VRRVAGGVVS NFVHDNLKVG DIVGVSPPAG NFVYKRSEEN VNRPLLCFAG
GIGITPLIPI IETALLDGRK VNFCYSSRNY VSRPFKQWLE QLKLKYKENL KLKEFFSEES
SVTKEQIVDE VMTRIINEED LEKLDLSECD IYMLGPNNYM RFVKQELVKL GVEPNKVQSE
FFGPYIP
