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CYSJ_VIBCH
ID   CYSJ_VIBCH              Reviewed;         614 AA.
AC   Q9KUX4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000255|HAMAP-Rule:MF_01541};
DE            Short=SiR-FP {ECO:0000255|HAMAP-Rule:MF_01541};
DE            EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01541};
GN   Name=cysJ {ECO:0000255|HAMAP-Rule:MF_01541}; OrderedLocusNames=VC_0384;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01541};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01541};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01541};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC       sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC       beta component is a hemoprotein. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC       flavoprotein subunit CysJ family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
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DR   EMBL; AE003852; AAF93557.1; -; Genomic_DNA.
DR   PIR; B82329; B82329.
DR   RefSeq; NP_230038.1; NC_002505.1.
DR   AlphaFoldDB; Q9KUX4; -.
DR   SMR; Q9KUX4; -.
DR   STRING; 243277.VC_0384; -.
DR   DNASU; 2615027; -.
DR   EnsemblBacteria; AAF93557; AAF93557; VC_0384.
DR   KEGG; vch:VC_0384; -.
DR   PATRIC; fig|243277.26.peg.360; -.
DR   eggNOG; COG0369; Bacteria.
DR   HOGENOM; CLU_001570_17_7_6; -.
DR   OMA; QKRYQRD; -.
DR   BioCyc; VCHO:VC0384-MON; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000000584; Chromosome 1.
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-UniRule.
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; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   HAMAP; MF_01541; CysJ; 1.
DR   InterPro; IPR010199; CysJ.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR029758; CysJ_Proteobact.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Electron transport; FAD;
KW   Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; Transport.
FT   CHAIN           1..614
FT                   /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT                   component"
FT                   /id="PRO_0000199939"
FT   DOMAIN          79..217
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   DOMAIN          249..463
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         85..90
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         132..135
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         168..177
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         371
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         401..404
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         419..421
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         425
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         434..437
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         534..535
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         540..544
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         576
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         614
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
SQ   SEQUENCE   614 AA;  67702 MW;  3081C655722FF44D CRC64;
     MNREVVTMST GNTLPPALAA LASPLNDAQL NQLQQTVTQL NAQQLAWVSG YFWGLSQSNA
     LSVPHISAGQ TASAASGKLT IIFASQTGNA KGVAQALLKE AQAAGIQAQL FDASDYKGKD
     LAKETHVIFV ASTNGEGEAP DNALALHEFL KSKKAPKLPN LKYGVLGLGD SSYQFFCQTG
     KDFDQFLENL GAQRLVERLD ADVDYQAAAT EWRKQVLSIL KDELTGAAAV TSVATFAVSQ
     TAESHYSKEQ PYTASLSTSQ KITGRDSGKD VRHIEIDLAD SGITYQPGDA LGVWYENRPQ
     LVNALLDSVG LSGHEEVQVD GETLSLHSAL THHYEITAAN PQLVAQFAEL AQSEKLTSLA
     QDKEALREYA TRTQVIDVLR EEKVTLSAIQ LLSLLRRLTP RLYSIASSQS EVGEEVHLTV
     GVVEYEYEGE QRLGGASSFL AHQLEEGAPV KVFVEHNNNF KLPSDDNAPL IMVGPGTGIA
     PFRSFIQERE NRGAAGKNWL LFGDRTFTQD FLYQVEWQKY LKSGVLNRLD VAFSRDQHEK
     VYVQHRLLEQ AELVWQWLQE GAYFYVCGDA SRMAKDVHQA LITVVEQQGG LNREQAEEYV
     SELRKAKRYQ RDVY
 
 
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