ID CYSJ_BAUCH Reviewed; 595 AA. AC Q1LTP1; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 02-SEP-2026, 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}; GN OrderedLocusNames=BCI_0218; OS Baumannia cicadellinicola subsp. Homalodisca coagulata. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Candidatus Palibaumannia. OX NCBI_TaxID=374463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188; RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.; RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of RT sharpshooters."; RL PLoS Biol. 4:1079-1092(2006). 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=hydrogen sulfide + 3 NADP(+) + 3 H2O = sulfite + 3 NADPH + 4 CC H(+); 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; Evidence={ECO:0000255|HAMAP- CC 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000238; ABF14003.1; -; Genomic_DNA. DR RefSeq; WP_011520406.1; NC_007984.1. DR AlphaFoldDB; Q1LTP1; -. DR SMR; Q1LTP1; -. DR STRING; 374463.BCI_0218; -. DR KEGG; bci:BCI_0218; -. DR HOGENOM; CLU_001570_17_7_6; -. DR OrthoDB; 9816402at2; -. DR UniPathway; UPA00140; UER00207. DR Proteomes; UP000002427; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019344; P:L-cysteine biosynthetic process; IEA:InterPro. DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule. DR CDD; cd06199; SiR; 1. DR FunFam; 3.40.50.80:FF:000001; NADPH--cytochrome P450 reductase 1; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 1.20.990.10; NADPH-cytochrome p450 Reductase, Chain A, domain 3; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 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 NCBIfam; TIGR01931; cysJ; 1. DR NCBIfam; NF008197; PRK10953.1; 1. DR PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. 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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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..595 FT /note="Sulfite reductase [NADPH] flavoprotein alpha- FT component" FT /id="PRO_0000292965" FT DOMAIN 59..197 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT DOMAIN 230..444 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 65..70 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 112..115 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 148..157 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 318 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 352 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 382..385 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 400..402 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 406 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 415..418 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 515..516 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 521..525 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 557 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" FT BINDING 595 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541" SQ SEQUENCE 595 AA; 67733 MW; F6F314B06CE8CAAC CRC64; MTQQNAPKDL PPLSAEQLDR LQAISSDLSN LQLAWASGYL WNKASHSIPI DYTASQQVIT VLSASQTGNA RRLAVQLYED LLAAQLSVVI INAGDYKFKQ IAQEKWLLIV TSTQGDGDPP EEAIALYKYL FSKKAPVLNN IQFAIFGLGD SSYTYFAKIG KDFDSRLAEL GAQRLYDRVD ADVDYQEKAD IWRREIVKIL QTKLVTVNAK QQLSVINNRI EVKNNLYTKE EPFTAHLVVK QKITSRSSKK DIRHLEIDIA GSGLNYQPGD ALGVWYENDP VLISEILELL GLTGNELVQV KEKNIPLNEA LQKHYELTNN TAEIVKSYAY ITRNSSLLAL VDDQQQLKQF AFSTPFIDMI QRIPVELHPK QLLTLLRPLM PRLYSIASSQ AEVGDEVHLT VSVVRYEIDG KIRTGGASSY LAYRLQESEP IRVFIEHNDN FRLPNNPNTA IIMIGSGTGI APFRGFMQQR EATTAKGKNW LFFGNQHLTD DFLYQVEWQR YIKNGLLNKI DVAWSQDQNK KIYVQDRLLE KGIELWNWIQ DGAHIYVCGN ANLMARDVEK ALVKLIAIHG RMDYEQADEF LSELRIARRF QRDTY //