ID A0A3S9UZH7_9BACL Unreviewed; 633 AA.
AC A0A3S9UZH7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Assimilatory sulfite reductase (NADPH) flavoprotein subunit {ECO:0000313|EMBL:AZS15706.1};
DE EC=1.8.1.2 {ECO:0000313|EMBL:AZS15706.1};
GN ORFNames=EI981_15490 {ECO:0000313|EMBL:AZS15706.1};
OS Paenibacillus lutimineralis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS15706.1, ECO:0000313|Proteomes:UP000270678};
RN [1] {ECO:0000313|Proteomes:UP000270678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT "Complete genome sequence of Paenibacillus sp. MBLB1234.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
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DR EMBL; CP034346; AZS15706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9UZH7; -.
DR KEGG; plut:EI981_15490; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000270678; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
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 Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000207-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000207-1};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000207-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AZS15706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270678};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 89..227
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 263..482
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 95..100
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 142..145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 178..187
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 420..423
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 444
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 453..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 553..554
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 559..563
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 595
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 633
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ SEQUENCE 633 AA; 70095 MW; A6CCC87DBA4BF612 CRC64;
MVLQVTNSPF NEEQVDLLNR LLPGLNDSQR LWLSGYLTAL LGTAAGEAAP IASTAAGQTV
TVSTADSAIP AASELSSAVQ LGAPVSKEVT VLYGSQTGNA KGLAQQLSRR LEGEGLKVTT
VSMGDLKPNQ LKKIERLVLL VSTHGEGEPP DAAISFYEFL HSKRAPKLEG LEFSVLALGD
TSYEFFCQTG KDFDQRLEEL GGKRIVERAD CDVDYDETAT EWTNQVLAAL NVGHAVAAGT
IQVNSSQVTG GLADGDSSAY SRTNPFKAEI LENLNLNGRG SERETRHIEL SLEGSGLQYQ
PGDCLAIYPE NHPQLVQDIL EAMGWSGEQL VTFNKNGEQK SLRDALLTHY EITVLTKPLL
TQAAALTGHA QLQQLIQVGH EAELKSYLNR RDLLDLIQDF SLKGHTAQEI TSILRKIPPR
QYSISSSPTA YPEEVHITVR TVNYESYGRE RYGVCSTQLA QRAEVGEHLP VYIQQNDQFR
LPDNPDTPII MIGPGTGVAP FRAFLGEREE AGATGKSWLF YGDQHFITDF LYQIEWQRWL
KDGVLTRMDV AFSRDTAEKV YVQHRMLEHS RELFAWLEEG AVVYVCGDEK RMAHDVQTTL
LQIIEREGAL NSEQAAQYLA GMQQEKRYLR DVY
//
