CYSJ_BACSU
ID CYSJ_BACSU Reviewed; 605 AA.
AC O32214;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE Short=SiR-FP;
DE EC=1.8.1.2;
GN Name=cysJ; Synonyms=yvgR; OrderedLocusNames=BSU33440;
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 The flavoprotein component catalyzes the electron flow from NADPH ->
CC FAD -> FMN to the hemoprotein component (Probable).
CC {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=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 -!- 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}.
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DR EMBL; AL009126; CAB15349.1; -; Genomic_DNA.
DR PIR; G70040; G70040.
DR RefSeq; NP_391224.1; NC_000964.3.
DR RefSeq; WP_003243259.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32214; -.
DR SMR; O32214; -.
DR STRING; 224308.BSU33440; -.
DR PaxDb; O32214; -.
DR PRIDE; O32214; -.
DR EnsemblBacteria; CAB15349; CAB15349; BSU_33440.
DR GeneID; 936022; -.
DR KEGG; bsu:BSU33440; -.
DR PATRIC; fig|224308.179.peg.3629; -.
DR eggNOG; COG0369; Bacteria.
DR InParanoid; O32214; -.
DR OMA; QKRYQRD; -.
DR PhylomeDB; O32214; -.
DR BioCyc; BSUB:BSU33440-MON; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR010199; CysJ.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000207; SiR-FP_CysJ; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR01931; cysJ; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Electron transport; FAD;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..605
FT /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT component"
FT /id="PRO_0000388469"
FT DOMAIN 68..206
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 235..454
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..78
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 121..126
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 154..185
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 392..395
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 525..533
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 605 AA; 67259 MW; 486F512C0AED6217 CRC64;
MQLQVMNSPF NQEQAELLNR LLPTLTESQK IWLSGYLSAQ SVSAQEAAGT PAAAVSAEAP
APAVSKEVTV LYGSQTGNAQ GLAENAGKQL EQSGFQVTVS SMSDFKPNQL KKVTNLLIVV
STHGEGEPPD NALSFHEFLH GRRAPKLEDL RFSVLALGDS SYEFFCQTGK EFDQRLEELG
GKRISPRVDC DLDYDEPAAE WLEGVLKGLN EAGGGSAAPA PAAASQTGES SYSRTNPFRA
EVLENLNLNG RGSNKETRHV ELSLEGSGLT YEPGDSLGVY PENDPELVEL LLKEMNWDPE
EIVTLNKQGD VRPLKEALIS HYEITVLTKP LLEQAAQLTG NDELRELLAP GNEENVKAYI
EGRDLLDLVR DYGPFSVSAQ EFVSILRKMP ARLYSIASSL SANPDEVHLT IGAVRYDAHG
RERKGVCSIL CAERLQPGDT LPVYVQHNQN FKLPKDPETP IIMVGPGTGV APFRSFMQER
EETGAEGKAW MFFGDQHFVT DFLYQTEWQN WLKDGVLTKM DVAFSRDTEE KVYVQHRMLE
HSAELFEWLQ EGAAVYICGD EKHMAHDVHN TLLEIIEKEG NMSREEAEAY LADMQQQKRY
QRDVY
