MET5_SCHPO
ID MET5_SCHPO Reviewed; 1473 AA.
AC Q1K9C2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sulfite reductase [NADPH] subunit beta;
DE EC=1.8.1.2;
GN Name=sir1; ORFNames=SPAC10F6.01c, SPAC4C5.05c;
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:CAB11176.1}
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: Catalyzes the reduction of sulfite to sulfide, one of several
CC activities required for the biosynthesis of L-cysteine from sulfate.
CC {ECO:0000250|UniProtKB:P47169}.
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 Evidence={ECO:0000250|UniProtKB:P47169};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000250|UniProtKB:P17846};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250|UniProtKB:P17846};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P17846};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P17846};
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 (By similarity).
CC {ECO:0000250|UniProtKB:P47169}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000255}.
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DR EMBL; CU329670; CAB11176.1; -; Genomic_DNA.
DR RefSeq; NP_593252.1; NM_001018649.2.
DR AlphaFoldDB; Q1K9C2; -.
DR SMR; Q1K9C2; -.
DR BioGRID; 279361; 7.
DR STRING; 4896.SPAC10F6.01c.1; -.
DR iPTMnet; Q1K9C2; -.
DR SwissPalm; Q1K9C2; -.
DR MaxQB; Q1K9C2; -.
DR PaxDb; Q1K9C2; -.
DR PRIDE; Q1K9C2; -.
DR EnsemblFungi; SPAC10F6.01c.1; SPAC10F6.01c.1:pep; SPAC10F6.01c.
DR GeneID; 2542920; -.
DR KEGG; spo:SPAC10F6.01c; -.
DR PomBase; SPAC10F6.01c; sir1.
DR VEuPathDB; FungiDB:SPAC10F6.01c; -.
DR eggNOG; KOG0560; Eukaryota.
DR HOGENOM; CLU_001975_1_0_1; -.
DR InParanoid; Q1K9C2; -.
DR OMA; GMGATHN; -.
DR PhylomeDB; Q1K9C2; -.
DR UniPathway; UPA00140; UER00207.
DR PRO; PR:Q1K9C2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); ISO:PomBase.
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; IMP:PomBase.
DR GO; GO:0000103; P:sulfate assimilation; IMP:PomBase.
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.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..1473
FT /note="Sulfite reductase [NADPH] subunit beta"
FT /id="PRO_0000316860"
FT DOMAIN 728..876
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 1328
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P17846"
FT BINDING 1334
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P17846"
FT BINDING 1373
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P17846"
FT BINDING 1377
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P17846"
FT BINDING 1377
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|UniProtKB:P17846"
SQ SEQUENCE 1473 AA; 163844 MW; A9A310E7310DF1F2 CRC64;
MSVKASINNS QEAVSRIAFR CSDALYVVHP NNSILNGALT ESLKDLKKFE TLNVSGKVPH
VLPLKSHADP FAHIADAILA EEEVASTQPK QITSVVASAD ALFFATPHLY KLAHEPLVAH
VAIESTEAFD FASVRDTGFV ILFSGNRPGD SSEAALEDTL ETASLAHRLA LKLNTGVLHF
YSPVYDTTAA LENIETLPSK EDAQHARVAH IPIEEKQEDS EKEGNIKEAF VPPKFDQPER
DAATSEYLES LSIKPFEYSG SDDATDVLLV FGSAASELAK AAVTSSVAVA IVRVLRPWLP
SKLQEVLPTS TKRLTVLEPI TSLPRKWDPL YLDVLSSFVA SGSSIELFAV RYGLSSSEQA
TEIIKAVRDN LSGALKPSLV CDFTDGVSQV FVPTPPSIEE AYHKLLHRVF KSRLNIVNDP
ASSATKQNIP SRLIISPQFA LGSVLEYENQ RRAFCDEVAT LLKEKNSSVS SESLEVLSNW
IVSVDNLESP VDPELVISEL KKDSSAPIKS LLDRSEFFTN VSHWIIGSDA WAYDLGNSAL
HQVLCLEKNV NLLIVDTQPY STREAVRSSS RKKDIGLYAM NFGNAYVAST ALYSSYTQLI
SALLEADKFK GPSVVLAYLP YHSADDDAIT VLQETKKAVD IGYWPLYRWT PALEDGEYSD
FKLDSERIRR ELKTFLERDN YLTQLTLRVP SLARTLTQSF GAEVRHQQNV DSRNALNKLI
EGLSGPPLTI LFASDGGTAE NVAKRLQNRA SARGSKCKIM AMDDFPIEEL GNEKNVVVLV
STAGQGEFPQ NGREFWEAIK GADLNLSELK YGVFGFGDYE YWPRKEDKIY YNRPGKQLDA
RFVELGAAPL VTLGLGNDQD PDGWETAYNL WEPELWKALG LDNVEIDIDE PKPITNEDIK
QASNFLRGTI FEGLADESTG ALAESDCQLT KFHGIYMQDD RDIRDERKKQ GLEPAYGFMI
RARMPAGVCT PEQWIAMDDI STKWGNHTLK ITTRQTFQWH GVLKKNLRNT IRNIVKVFLT
TLGACGDVAR NVTCSSTPNN ETIHDQLFAV SKQISNELLP TTSSYHEIWI EDPETVEKRK
VAGEAVQDVE PLYGPTYLPR KFKVGVAAPP YNDVDVYTND VALIAIIEND KVLGFNVGIG
GGMGTTHNNK KTYPRLATVV GYVLTDKIME VVKAILIVQR DNGDRENRKH ARLKYTVDTL
GVSTFVEKVE EVLGYKFEEA RDHPQFIKNH DDFEGWHKTE KNKYWRSIFV ENGRIENNGI
LQFKTGLREL AERLYTEKSE AEFRLTANQH VILFNVAENE LGWINEHMAK YKLDNNAFSG
LRLSSAACVA LPTCGLAMAE SERYLPKLIT KVEEIVYEAG LQKDSIVMRM TGCPNGCSRP
WVAEIACVGK APNTYNLMLG GGFYGQRLNK LYRSSVQEKE ILNLLRPLIK RYALEREDGE
HFGDWVIRAG IITAVENGGA NGAVHEGVSP EAF
