ID   MET10_SCHPO             Reviewed;        1006 AA.
AC   Q09878;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Probable sulfite reductase [NADPH] flavoprotein component;
DE            EC=1.8.1.2;
GN   ORFNames=SPCC584.01c;
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]
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).
CC   -!- FUNCTION: This enzyme catalyzes the 6-electron reduction of sulfite to
CC       sulfide. This is one of several activities required for the
CC       biosynthesis of L-cysteine from sulfate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC         sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.8.1.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC       sulfide from sulfite (NADPH route): step 1/1.
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DR   EMBL; CU329672; CAA21818.2; -; Genomic_DNA.
DR   PIR; T41439; T41439.
DR   RefSeq; NP_588222.1; NM_001023212.2.
DR   AlphaFoldDB; Q09878; -.
DR   SMR; Q09878; -.
DR   BioGRID; 275402; 42.
DR   STRING; 4896.SPCC584.01c.1; -.
DR   iPTMnet; Q09878; -.
DR   MaxQB; Q09878; -.
DR   PaxDb; Q09878; -.
DR   PRIDE; Q09878; -.
DR   EnsemblFungi; SPCC584.01c.1; SPCC584.01c.1:pep; SPCC584.01c.
DR   GeneID; 2538821; -.
DR   KEGG; spo:SPCC584.01c; -.
DR   PomBase; SPCC584.01c; -.
DR   VEuPathDB; FungiDB:SPCC584.01c; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_003662_1_0_1; -.
DR   InParanoid; Q09878; -.
DR   OMA; FRIWEED; -.
DR   PhylomeDB; Q09878; -.
DR   UniPathway; UPA00140; UER00207.
DR   PRO; PR:Q09878; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); ISO:PomBase.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; ISO:PomBase.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; ISO:PomBase.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   Gene3D; 3.40.920.10; -; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase;
KW   Reference proteome; Transport.
FT   CHAIN           1..1006
FT                   /note="Probable sulfite reductase [NADPH] flavoprotein
FT                   component"
FT                   /id="PRO_0000199948"
FT   DOMAIN          622..852
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         658..669
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         788..798
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1006 AA;  111353 MW;  2EA2086D69561D33 CRC64;
     MVATDSSDQV AKFDVSHKII EDIVYSLSNR IFSYAEHVPL NRYLTQWNNS GRRNGFSNNV
     ELFNLEARSG ASAFLLGSYT AAISSPGVYS MMTPSSCLSL LNPLLSNIIP FYGASKPLVV
     HVAALAYLEQ TYCADNVSVL DFSYANNFTV FASQSNVEAA HLALASTLAA KAAPVIHVYE
     PDAIVTTTDP SLPLLDSNAV VECFNSYQSE ADPVSNASKA LKHVNDYFNT SYAPAEYYGS
     QTASKVIVTF GKSETVAARA LLAANPDVGV LSIRIFPFVA ENIFNVLPTT CKSLVVLSQV
     RSTAVGTSSI YYSFLLATLL STKPSALAIS EHRYSLVESV TLSSLFDALH ETLQLKAATP
     KAVHVDKSIN VWESDVGDSL VLSLVSAYRT DKSRSVAFRP LFDNLTLAGV RFTVAQVSTA
     NAVLTDVVKD VDADITILTT DRLPLHYRVL AKAAEHSICL LQSSIAPDEA TKKLPYEFIA
     DALEKGVKLV LIDPKKFAID ASNLPLLVSF IQLVKPGLGV DEALAVLAKQ NNLTDTNLKD
     AVDSLKQSLS FINLDASALK DREPSEKELP STAKETSFAP NAVKTLDEDI TPQSSNWQTV
     AKQIIFPEAY KKKDALRPDV SEKVFTVHVR ANKRLTPAEY NRNIFHIEFD LGDSGLTYDI
     GEALGVYGVN NKTHVHDFIE EYGLDANELI HVPSIQHPGH WETRTVFQAL CQNIDIFGKP
     TKKFHEQLLE FETDEKERAD LQILISPAGA PDFKRRAEVD MLTYADVLKE FKHAKLTAAQ
     IAQIVPVIKR REYSISSSQK KHNDSVHLLV VVVGWKDGMG RDRYGQCSHY LSNLKVGEPL
     CVAVKTSVMK LPTSPLKPIV MAGLGTGLAP FRAFLQFKEW QRMQGIESGD ILLYLGSRTQ
     REEYLYGEDW EAYHSANLLT HIGQAFSRDQ PYKIYIQDVM RSTKDMLKKA LMDEGGSFYL
     CGPTWPLPEI TSVLEEVIQS SYDEPVDARK IIEQWKEERR FVIEVY