MET5_YEAST
ID MET5_YEAST Reviewed; 1442 AA.
AC P47169; D6VWV6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Sulfite reductase [NADPH] subunit beta;
DE EC=1.8.1.2;
DE AltName: Full=Extracellular mutant protein 17;
GN Name=MET5; Synonyms=ECM17; OrderedLocusNames=YJR137C; ORFNames=J2126;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
RA Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
RA Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
RT "Linking genome and proteome by mass spectrometry: large-scale
RT identification of yeast proteins from two dimensional gels.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
RN [5]
RP IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, one of several
CC activities required for the 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=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1.
CC -!- SUBUNIT: Alpha(2)-beta(2). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; Z49637; CAA89669.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08922.1; -; Genomic_DNA.
DR PIR; S57160; S57160.
DR RefSeq; NP_116579.1; NM_001181795.1.
DR AlphaFoldDB; P47169; -.
DR SMR; P47169; -.
DR BioGRID; 33893; 143.
DR ComplexPortal; CPX-3163; Sulfite reductase complex (NADPH).
DR IntAct; P47169; 8.
DR STRING; 4932.YJR137C; -.
DR CarbonylDB; P47169; -.
DR iPTMnet; P47169; -.
DR MaxQB; P47169; -.
DR PaxDb; P47169; -.
DR PRIDE; P47169; -.
DR EnsemblFungi; YJR137C_mRNA; YJR137C; YJR137C.
DR GeneID; 853602; -.
DR KEGG; sce:YJR137C; -.
DR SGD; S000003898; MET5.
DR VEuPathDB; FungiDB:YJR137C; -.
DR eggNOG; KOG0560; Eukaryota.
DR HOGENOM; CLU_001975_2_1_1; -.
DR InParanoid; P47169; -.
DR OMA; CSRPWLA; -.
DR BioCyc; YEAST:MON3O-22; -.
DR UniPathway; UPA00140; UER00207.
DR PRO; PR:P47169; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47169; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
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; IMP:SGD.
DR Gene3D; 3.30.413.10; -; 2.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
DR SUPFAM; SSF55124; SSF55124; 2.
DR SUPFAM; SSF56014; SSF56014; 2.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..1442
FT /note="Sulfite reductase [NADPH] subunit beta"
FT /id="PRO_0000199968"
FT DOMAIN 682..831
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 1300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1306
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1345
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1349
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1349
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1442 AA; 161219 MW; E34695088BA9FE94 CRC64;
MTASDLLTLP QLLAQYSSSA PQNKVFYTTS TKNSHSSFKG LESVATDATH LLNNQDPLNT
IKDQLSKDIL TTVFTDETTL VKSIHHLYSL PNKLPLVITV DLNLQDYSAI PALKDLSFPI
LISSDLQTAI SNADSSYKIA TSSLTPVFHF LNLEKIGTST AIEQDIDFPT LEIANEETKV
ALSEATDSLT NFELVKGKES ITTVIVNLSP YDAEFSSVLP SNVGLIKIRV YRPWNFSKFL
EILPSSVTKI AVLQGVSKKS QSNEFQPFLL DFFGNFNELV SRNIEQVVLT NIGNVNDYGN
VINTVISNIN KKEPDNNLFL GESNEKAEEQ AEVTQLISSV KKVVNLEDAY IKVLKQLFSS
NLQILNQFSS ETIEPSNPEF GFGRFLKQEA QREELISLAK TSLDPSLYLS EDANKIVQLL
SKWLSFNGRD LDEAQLQEAN ATGLEIFQLL QSNQDSSTVL KFLKIAPTSD SFIFKSSWLI
GSDAWSYDLG HSGIQQVLSS RKNINVLLID SEPYDHRKQN QDRKKDVGLY AMNYYSAYVA
SVAVYASYTQ LLTAIIEASK YNGPSIVLAY LPYNSENDTP LEVLKETKNA VESGYWPLYR
FNPVYDDPST DKEAFSLDSS VIRKQLQDFL DRENKLTLLT RKDPSLSRNL KQSAGDALTR
KQEKRSKAAF DQLLEGLSGP PLHVYYASDG GNAANLAKRL AARASARGLK ATVLSMDDII
LEELPGEENV VFITSTAGQG EFPQDGKSFW EALKNDTDLD LASLNVAVFG LGDSEYWPRK
EDKHYFNKPS QDLFKRLELL SAKALIPLGL GDDQDADGFQ TAYSEWEPKL WEALGVSGAA
VDDEPKPVTN EDIKRESNFL RGTISENLKD TSSGGVTHAN EQLMKFHGIY TQDDRDIREI
RKSQGLEPYY MFMARARLPG GKTTPQQWLA LDHLSDTSGN GTLKLTTRAT FQIHGVLKKN
LKHTLRGMNA VLMDTLAAAG DVNRNVMVSA LPTNAKVHQQ IADMGKLISD HFLPKTTAYH
EVWLEGPEEQ DDDPSWPSIF ENRKDGPRKK KTLVSGNALV DIEPIYGPTY LPRKFKFNIA
VPPYNDVDVL SIDVGLVAIV NPETQIVEGY NVFVGGGMGT THNNKKTYPR LGSCLGFVKT
EDIIPPLEGI VIVQRDHGDR KDRKHARLKY TVDDMGVEGF KQKVEEYWGK KFEPERPFEF
KSNIDYFGWI KDETGLNHFT AFIENGRVED TPDLPQKTGI RKVAEYMLKT NSGHFRLTGN
QHLVISNITD EHVAGIKSIL KTYKLDNTDF SGLRLSSSSC VGLPTCGLAF AESERFLPDI
ITQLEDCLEE YGLRHDSIIM RMTGCPNGCS RPWLGELALV GKAPHTYNLM LGGGYLGQRL
NKLYKANVKD EEIVDYIKPL FKRYALEREE GEHFGDFCIR VGIIKPTTEG KYFHEDVSED
AY
