FMNR_SCHPO
ID FMNR_SCHPO Reviewed; 200 AA.
AC Q9USJ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NAD(P)H-dependent FMN reductase C4B3.06c;
DE Short=FMN reductase C4B3.06c;
DE EC=1.5.1.39;
DE AltName: Full=Azoreductase C4B3.06c;
DE AltName: Full=FMN reductase [NAD(P)H];
GN ORFNames=SPCC4B3.06c;
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:CAB60680.1}
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: Has several reductase activities that are NAD(P)H-dependent
CC and involve FMN as a cofactor. May be involved in ferric iron
CC assimilation (By similarity). {ECO:0000250|UniProtKB:Q07923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.39;
CC Evidence={ECO:0000250|UniProtKB:Q07923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.39;
CC Evidence={ECO:0000250|UniProtKB:Q07923};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q07923}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAB60680.1; -; Genomic_DNA.
DR PIR; T50442; T50442.
DR RefSeq; NP_588084.1; NM_001023076.2.
DR AlphaFoldDB; Q9USJ6; -.
DR SMR; Q9USJ6; -.
DR BioGRID; 275302; 5.
DR STRING; 4896.SPCC4B3.06c.1; -.
DR MaxQB; Q9USJ6; -.
DR PaxDb; Q9USJ6; -.
DR EnsemblFungi; SPCC4B3.06c.1; SPCC4B3.06c.1:pep; SPCC4B3.06c.
DR GeneID; 2538718; -.
DR KEGG; spo:SPCC4B3.06c; -.
DR PomBase; SPCC4B3.06c; -.
DR VEuPathDB; FungiDB:SPCC4B3.06c; -.
DR eggNOG; KOG4530; Eukaryota.
DR HOGENOM; CLU_055322_2_1_1; -.
DR InParanoid; Q9USJ6; -.
DR OMA; AIDWHFT; -.
DR PhylomeDB; Q9USJ6; -.
DR PRO; PR:Q9USJ6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; ISO:PomBase.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Flavoprotein; FMN; NAD; NADP; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..200
FT /note="NAD(P)H-dependent FMN reductase C4B3.06c"
FT /id="PRO_0000315910"
FT BINDING 22
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07923"
FT BINDING 96..99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07923"
FT BINDING 126
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07923"
SQ SEQUENCE 200 AA; 22125 MW; D9552E192A940C98 CRC64;
MTLPEKLLKI TPKILVIMGS VRSKRLCPTI ATWVGEMGKR ETNFDYEKVD LTDWPLSMSD
EPGLPIMGID VYTQEHTKAW GSKIAGADGF VFVTPQYNGG YPAILKNALD HLYHEWNGKP
LLIVSYGGHG GGDCASQLKH VAGFLKMRVA PTMPALTLPR DKIVQGVVDP AVEFTKHLGE
LKKAFGEFSQ LFESNPERKP
