MET10_YEAST
ID MET10_YEAST Reviewed; 1035 AA.
AC P39692; D6VTR0; Q12683;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein component;
DE EC=1.8.1.2;
GN Name=MET10; OrderedLocusNames=YFR030W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7928966; DOI=10.1128/jb.176.19.6050-6058.1994;
RA Hansen J., Cherest H., Kielland-Brandt M.C.;
RT "Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from
RT Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase
RT and specify potential binding sites for FAD and NADPH.";
RL J. Bacteriol. 176:6050-6058(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-16 AND 684-707,
RP AND INDUCTION.
RX PubMed=7788524; DOI=10.1093/dnares/2.1.15;
RA Hosseini-Mazinani S.M., Koshikawa N., Sugimoto K., Aoki Y., Arisawa M.;
RT "Cloning and sequencing of sulfite reductase alpha subunit gene from
RT Saccharomyces cerevisiae.";
RL DNA Res. 2:15-19(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1015-1035.
RX PubMed=7698648; DOI=10.1101/gad.9.5.587;
RA Strunnikov A.V., Hogan E., Koshland D.;
RT "SMC2, a Saccharomyces cerevisiae gene essential for chromosome segregation
RT and condensation, defines a subgroup within the SMC family.";
RL Genes Dev. 9:587-599(1995).
RN [7]
RP CHARACTERIZATION.
RX PubMed=6751400; DOI=10.1016/0167-4838(82)90257-6;
RA Kobayashi K., Yoshimoto A.;
RT "Studies on yeast sulfite reductase. IV. Structure and steady-state
RT kinetics.";
RL Biochim. Biophys. Acta 705:348-356(1982).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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.
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.
CC -!- INDUCTION: By methionine deprivation. {ECO:0000269|PubMed:7788524}.
CC -!- MISCELLANEOUS: Present with 1580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L26503; AAA61982.1; -; Genomic_DNA.
DR EMBL; D44610; BAA08076.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09269.1; -; Genomic_DNA.
DR EMBL; U05820; AAA17417.2; -; Genomic_DNA.
DR EMBL; BK006940; DAA12470.1; -; Genomic_DNA.
DR PIR; S56285; S56285.
DR RefSeq; NP_116686.3; NM_001179995.3.
DR AlphaFoldDB; P39692; -.
DR SMR; P39692; -.
DR BioGRID; 31185; 95.
DR ComplexPortal; CPX-3163; Sulfite reductase complex (NADPH).
DR DIP; DIP-6609N; -.
DR IntAct; P39692; 21.
DR MINT; P39692; -.
DR STRING; 4932.YFR030W; -.
DR MaxQB; P39692; -.
DR PaxDb; P39692; -.
DR PRIDE; P39692; -.
DR EnsemblFungi; YFR030W_mRNA; YFR030W; YFR030W.
DR GeneID; 850588; -.
DR KEGG; sce:YFR030W; -.
DR SGD; S000001926; MET10.
DR VEuPathDB; FungiDB:YFR030W; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_1_0_1; -.
DR InParanoid; P39692; -.
DR OMA; EEKLWQK; -.
DR BioCyc; MetaCyc:MON3O-21; -.
DR BioCyc; YEAST:MON3O-21; -.
DR UniPathway; UPA00140; UER00207.
DR PRO; PR:P39692; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P39692; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IDA:SGD.
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; IEA:UniProtKB-EC.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IMP:SGD.
DR GO; GO:0000097; P:sulfur amino acid biosynthetic process; IC:ComplexPortal.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.40.50.920; -; 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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; FMN;
KW NADP; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..1035
FT /note="Sulfite reductase [NADPH] flavoprotein component"
FT /id="PRO_0000199947"
FT DOMAIN 648..879
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 684..695
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 814..824
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="A -> T (in Ref. 2; BAA08076)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="A -> G (in Ref. 1; AAA61982)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="M -> V (in Ref. 1; AAA61982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1035 AA; 114829 MW; 924B4047D645E1C3 CRC64;
MPVEFATNPF GEAKNATSLP KYGTPVTAIS SVLFNNVDSI FAYKSFSQPD LLHQDLKKWS
EKRGNESRGK PFFQELDIRS GAGLAPLGFS HGLKNTTAIV APGFSLPYFI NSLKTVSHDG
KFLLNVGALN YDNATGSVTN DYVTALDAAS KLKYGVVTPI SANEVQSVAL LALAIATFSN
NSGAINLFDG LNYSKTVLPL VESVPEASIL AKLSKVIAPD AAFDDVLDKF NELTGLRLHN
FQYFGAQDAE TVFITYGSLE SELFNSAISG NNSKIGLINV RVPLPFNVAK FVTHVPSTTK
QIVVIGQTLD GSSPSFLRSQ VSAALFYHGR TSISVSEYIY QPDFIWSPKA VKSIVSSFIP
EFTYNADSSF GEGFIYWASD KSINIDVASK LVKALSLEDG KFVSLRTKFD NLANAGTFQA
QFVTSKEQIP VSNIDSTKLS VVEDVSLLKH LDVAATVAEQ GSIALVSQKA VKDLDLNSVE
SYVKNLGIPE SFLISIAKKN IKLFIIDGET TNDESKLSLF IQAVFWKLAF GLDVAECTNR
IWKSIDSGAD ISAASISEFL TGAFKNFLSE VPLALYTKFS EINIEKKEDE EEPAALPIFV
NETSFLPNNS TIEEIPLPET SEISDIAKKL SFKEAYEVEN KLRPDLPVKN FVVKVKENRR
VTPADYDRYI FHIEFDISGT GMTYDIGEAL GIHARNNESL VKEFLTFYGL NESDVVLVPN
KDNHHLLETR TVLQAFVENL DIFGKPPKRF YESLIPYASN EEEKKKLEDL VTPAGAVDLK
RFQDVEYYTY ADIFELFPSV RPSLEELVTI IEPLKRREYS IASSQKVHPN EVHLLIVVVD
WVDNKGRKRY GQASKYISDL AVGSELVVSV KPSVMKLPPS PKQPVIMSGL GTGLAPFKAI
VEEKLWQKQQ GYEIGEVFLY LGSRHKREEY LYGELWEAYK DAGIITHIGA AFSRDQPQKI
YIQDRIKENL DELKTAMIDN KGSFYLCGPT WPVPDITQAL QDILAKDAEE RGIKVDLDAA
IEELKEASRY ILEVY
