CYSI_BACSU
ID CYSI_BACSU Reviewed; 571 AA.
AC O32213;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE Short=SiR-HP;
DE Short=SiRHP;
DE EC=1.8.1.2;
GN Name=cysI; Synonyms=yvgQ; OrderedLocusNames=BSU33430;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN SULFATE ASSIMILATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=168 / BGSC1A1;
RX PubMed=11445163; DOI=10.1111/j.1574-6968.2001.tb10728.x;
RA van der Ploeg J.R., Barone M., Leisinger T.;
RT "Functional analysis of the Bacillus subtilis cysK and cysJI genes.";
RL FEMS Microbiol. Lett. 201:29-35(2001).
RN [3]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=12169591; DOI=10.1128/jb.184.17.4681-4689.2002;
RA Guillouard I., Auger S., Hullo M.-F., Chetouani F., Danchin A.,
RA Martin-Verstraete I.;
RT "Identification of Bacillus subtilis CysL, a regulator of the cysJI operon,
RT which encodes sulfite reductase.";
RL J. Bacteriol. 184:4681-4689(2002).
CC -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC 6-electron reduction of sulfite to sulfide. This is one of several
CC activities required for the biosynthesis of L-cysteine from sulfate
CC (Probable). {ECO:0000305|PubMed:11445163}.
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(8)-beta(8). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by sulfate and the transcriptional regulator
CC CysL. {ECO:0000269|PubMed:11445163, ECO:0000269|PubMed:12169591}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking the cysIJ genes are unable to use
CC sulfate, sulfite or butanesulfonate as sole sulfur source, grow poorly
CC with sulfide, but can still grow with thiosulfate, cysteine or
CC methionine. {ECO:0000269|PubMed:11445163}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15348.1; -; Genomic_DNA.
DR PIR; F70040; F70040.
DR RefSeq; NP_391223.1; NC_000964.3.
DR RefSeq; WP_003243849.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32213; -.
DR SMR; O32213; -.
DR IntAct; O32213; 1.
DR MINT; O32213; -.
DR STRING; 224308.BSU33430; -.
DR PaxDb; O32213; -.
DR PRIDE; O32213; -.
DR EnsemblBacteria; CAB15348; CAB15348; BSU_33430.
DR GeneID; 938605; -.
DR KEGG; bsu:BSU33430; -.
DR PATRIC; fig|224308.179.peg.3628; -.
DR eggNOG; COG0155; Bacteria.
DR InParanoid; O32213; -.
DR OMA; MGMTHGD; -.
DR PhylomeDB; O32213; -.
DR BioCyc; BSUB:BSU33430-MON; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR Gene3D; 3.30.413.10; -; 2.
DR HAMAP; MF_01540; CysI; 1.
DR InterPro; IPR011786; CysI.
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; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 2.
DR SUPFAM; SSF56014; SSF56014; 2.
DR TIGRFAMs; TIGR02041; CysI; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron;
KW Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..571
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000388478"
FT BINDING 436
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 485
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"
SQ SEQUENCE 571 AA; 64810 MW; E9A695C9797D6564 CRC64;
MVTKILKAPD GSPSDVERIK KESDYLRGTL KEVMLDRISA GIPDDDNRLM KHHGSYLQDD
RDLRNERQKQ KLEPAYQFML RVRMPGGVST PEQWLVMDDL SQKYGNGTLK LTTRETFQMH
GILKWNMKKT IQTIHSALLD TIAACGDVNR NVMCASNPYQ SEIHSEVYEW SKKLSDDLLP
RTRAYHEIWL DEERVAGTPE EEVEPMYGPL YLPRKFKIGI AVPPSNDIDV FSQDLGFIAI
VEDGKLIGFN VAIGGGMGMT HGDTATYPQL AKVIGFCRPE QMYDVAEKTI TIQRDYGNRS
VRKNARFKYT VDRLGLENVK EELENRLGWS LEEAKPYHFD HNGDRYGWVE GIEDKWHFTL
FVEGGRITDY DDYKLMTGLR EIAKVHTGEF RLTANQNLMI ANVSSDKKEE ISALIEQYGL
TDGKHYSALR RSSMACVALP TCGLAMAEAE RYLPTLLDKI EEIIDENGLR DQEITIRMTG
CPNGCARHAL GEIGFIGKAP GKYNMYLGAA FDGSRLSKMY RENIGEADIL SELRILLSRY
AKEREEGEHF GDFVIRAGII KATTDGTNFH D
