ID A0A0E4CXU9_9BACL Unreviewed; 620 AA.
AC A0A0E4CXU9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000313|EMBL:CQR56739.1};
DE EC=1.8.1.2 {ECO:0000313|EMBL:CQR56739.1};
GN Name=cysJ {ECO:0000313|EMBL:CQR56739.1};
GN ORFNames=PRIO_4337 {ECO:0000313|EMBL:CQR56739.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR56739.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-2015) 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; LN831776; CQR56739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E4CXU9; -.
DR STRING; 483937.AMQ84_01235; -.
DR KEGG; pri:PRIO_4337; -.
DR PATRIC; fig|1073571.4.peg.4643; -.
DR HOGENOM; CLU_001570_17_7_9; -.
DR Proteomes; UP000033163; Chromosome I.
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:CQR56739.1}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 79..217
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 250..469
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 132..135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 168..177
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 407..410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 440..443
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 540..541
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 546..550
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 582
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 620
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ SEQUENCE 620 AA; 68946 MW; 7A9C9D4FC1061371 CRC64;
MLQLQVTNSP FNEEQVELLN RLLPTLTQTQ QIWLGGYISA LTLQGAAAVS AAAPAVLAAP
SASTAAAGGA AEPARSREVT VLFGSQTGNC QRLASSLSGK LKEQGFEITV SAMNSFKPNT
LKKVENLLIL VSTHGEGEPP DNARSFHEFL NSKRAPRLEH LRFSVLALGD TSYEFFCQTG
KDFDQRLEEL GGQRLIPRVD CDLDYDEPVA AWMEQVITAL NGAGSAPAIA EEAVLAAEHA
ESLQSAYSRN HPFHAEVLEN LNLNGRGSDR ETRHLELSLA GSNITFEPGD ALGVYPENHP
RLVEEIIAAM GWNPEEPVPL NKKGEEGTLR EALLRHYEIT VLSKPLLEQA AKLSPAAGLH
ELLLPDRAPQ LKEYIQGRDL LDLVQDFSPW DVPARSFVTI LRKLPARLYS IASSYNANPE
EVHFTVRAVR YESHGRERYG VCSVHCAERV QPGDTLPIYI QNNPNFKLPA NPEVPVIMIG
PGTGVAPFRS FLEEREEQDA EGKTWLFYGD RHFVTDFLYQ TDWQRMLKDG VLTKLDVAFS
RDTEEKVYVQ HRILEHSREL YTWLQEGAHV YVCGDEKHMA HDVHSALISV IQAEGGLSPE
AAAAYLDHLQ QEQRYQRDVY
//
