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Database: UniProt
Entry: M5D0G6_STEMA
LinkDB: M5D0G6_STEMA
Original site: M5D0G6_STEMA 
ID   M5D0G6_STEMA            Unreviewed;       509 AA.
AC   M5D0G6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE            EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN   Name=cysJ {ECO:0000313|EMBL:CCP16872.1};
GN   ORFNames=SMRA8_2664 {ECO:0000313|EMBL:CCP16872.1};
OS   Stenotrophomonas maltophilia RA8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=1118157 {ECO:0000313|EMBL:CCP16872.1, ECO:0000313|Proteomes:UP000012177};
RN   [1] {ECO:0000313|EMBL:CCP16872.1, ECO:0000313|Proteomes:UP000012177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA8 {ECO:0000313|EMBL:CCP16872.1,
RC   ECO:0000313|Proteomes:UP000012177};
RA   Linke B., Adamek M., Schwartz T.;
RT   "Stenotrophomonas maltophilia SKK35 and RA8 Genome sequencing: Analysis and
RT   Comparison of Viurlence genes.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCP16872.1}.
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DR   EMBL; CALM01000745; CCP16872.1; -; Genomic_DNA.
DR   RefSeq; WP_006370970.1; NZ_CALM01000745.1.
DR   AlphaFoldDB; M5D0G6; -.
DR   Proteomes; UP000012177; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
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; 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   PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 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   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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CCP16872.1}; Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          13..147
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          170..368
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   509 AA;  55710 MW;  B7663828FEAC7D67 CRC64;
     MNALPTSTPF SRLLVGFASE SGNARALAQR LGADLQPHAP QVLPFNDIDV ASLGHGDVLL
     AISSSFGDGE PPANGEQFFE TLRQTPTLSG LRYAVFGLGD TGYPSFCGFT KALDAALSER
     QAQPLLHRVD ADLGYEQFFQ QWQPVLGQVL DGDLDAGQDL HLQVTAYGED NAFAAPILER
     RRLNSSDPAA WHLQLDIAGS GMAYRAGDTL HVVPENDPAL LQALATWYGD TAAVAALHDR
     ELRLLSKGVL RELAKLGGSE VLKGLLKVSQ KRELEAYLHG LDLLDVLQDH ATPDSIPLVR
     LRELLSPRLP RAYSIASHPC DDQLSLCVRE VRYTLRGRER FGTATGSLLH GGDHARVYCR
     SNPGFHLPDT GEAPLLLVGT GTGIAPLMGL MQELQANACE REVHLVFGEK HSQHDYLYRE
     QLQDWRARGV LAGLHTAFSR DGAEKVYVQH VLQQRAAEVR DVLARDGHLY LCGNKSHLEG
     AVREAIDAIV GEGHWDALRC EGRTHCELY
//
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