ID A0A9X9HVP9_NEISU Unreviewed; 596 AA. AC A0A9X9HVP9; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 27-MAR-2024, entry version 3. DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000256|PIRNR:PIRNR000207}; DE Short=SiR-FP {ECO:0000256|PIRNR:PIRNR000207}; DE EC=1.8.1.2 {ECO:0000256|PIRNR:PIRNR000207}; GN ORFNames=KCG54_04220 {ECO:0000313|EMBL:UTG70522.1}; OS Neisseria subflava. OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=28449 {ECO:0000313|EMBL:UTG70522.1, ECO:0000313|Proteomes:UP001057296}; RN [1] {ECO:0000313|EMBL:UTG70522.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TT0077 {ECO:0000313|EMBL:UTG70522.1}; RA Li L., Mac Aogain M., Xu T., Jaggi T.K., Chan L.Y., Keir H.R., Dicker A.J., RA Qu J., Liu Y., Chen H.S., Koh M.S., Ong T.H., Lim A.Y.H., Abisheganaden J., RA Low T.B., Oliver B.G., Tan N.S., Fang M., Chalmers J.D., Chotirmall S.H.; RT "Characterizing Neisseria spp. as novel respiratory pathobionts in RT bronchiectasis."; RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|PIRNR:PIRNR000207}. 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:0000256|PIRNR:PIRNR000207}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRNR:PIRNR000207, CC ECO:0000256|PIRSR:PIRSR000207-1}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRNR:PIRNR000207, CC ECO:0000256|PIRSR:PIRSR000207-1}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|PIRNR:PIRNR000207, CC ECO:0000256|PIRSR:PIRSR000207-1}; CC Note=Binds 1 FMN per subunit. {ECO:0000256|PIRNR:PIRNR000207, CC ECO:0000256|PIRSR:PIRSR000207-1}; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen CC sulfide from sulfite (NADPH route): step 1/1. CC {ECO:0000256|PIRNR:PIRNR000207}. CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the CC beta component is a hemoprotein. {ECO:0000256|PIRNR:PIRNR000207}. 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; CP073115; UTG70522.1; -; Genomic_DNA. DR Proteomes; UP001057296; Chromosome. 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:InterPro. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd06199; SiR; 1. DR Gene3D; 3.40.50.360; -; 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 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 NCBIfam; TIGR01931; cysJ; 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 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, KW ECO:0000256|PIRNR:PIRNR000207}; KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192, KW ECO:0000256|PIRNR:PIRNR000207}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|PIRNR:PIRNR000207}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000207}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|PIRNR:PIRNR000207}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000207}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000207}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000207}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000207}. FT DOMAIN 58..196 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT DOMAIN 230..445 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT BINDING 64..69 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 111..114 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 147..156 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 319 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 353 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 383..386 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 401..403 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 416..419 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 516..517 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 522..526 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 558 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" FT BINDING 596 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1" SQ SEQUENCE 596 AA; 65029 MW; 559CF7B49E76047A CRC64; MSQANPLPPE LSVQLSALSP TQLAWLSGYC WAQSQGVSGV AAEPSALQTA ASTVSRRVLV LSASQTGNAR SVAESLHAKL QAAGVEARLS SASDFKSKTL PDGDIVLLVT STQGEGEPPE EALPLYKFIY GKKKPDLSKL TFAVLGLGDS SYPNFCQAGK DFDAKFAELG AGRLNDLGIC DLEFQTDADA WIAAVVPKVA ELTAQAASPS ISTAPNGSAT PSNDAVYTKE KPYTAILSVR QKITSRDAEK DVEHIEIDLS GSGLHYQAGD ALGVWPLNAG DLVQEILDLN QLSGNETVQL SDGRETDIRT ALTESADITQ NTPAFVQQYA ELTNNEELKT IAADKAQLDA YLAATPPVGV FAAHLHPLDA QTLYSLFRPQ TPRLYSIASA QDEVGEEVHL TVGVVRFNHH DHTYTGVASG YLGERLEEGS EIRVFVEPNP NFRLPQNGDT PIIMIGAGTG VAPFRSFMQQ RAANGDSGKN WLFFGNQRLA DDFLYQLEWS DWRKDGLLTR ADLAWSRQGE HKVYVQHKIT ERAAEVWNWL QQGAHIYVCG DAARMARDVE NALIEVIETQ GKLSRDEAED YLNDLREDKR YQRDVY //