ID   A0A366HL01_9BURK        Unreviewed;       734 AA.
AC   A0A366HL01;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Sulfite reductase (NADPH) flavoprotein alpha-component {ECO:0000313|EMBL:RBP42891.1};
GN   ORFNames=DFR37_10116 {ECO:0000313|EMBL:RBP42891.1};
OS   Eoetvoesiella caeni.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Eoetvoesiella.
OX   NCBI_TaxID=645616 {ECO:0000313|EMBL:RBP42891.1, ECO:0000313|Proteomes:UP000253628};
RN   [1] {ECO:0000313|EMBL:RBP42891.1, ECO:0000313|Proteomes:UP000253628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25520 {ECO:0000313|EMBL:RBP42891.1,
RC   ECO:0000313|Proteomes:UP000253628};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RBP42891.1}.
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DR   EMBL; QNRQ01000001; RBP42891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366HL01; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000253628; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06201; SiR_like2; 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; IPR017927; FAD-bd_FR_type.
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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR005625; PepSY-ass_TM.
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; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 1.
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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253628};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        289..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          335..468
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          484..597
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   734 AA;  79089 MW;  4EFD73CAB5092F82 CRC64;
     MSWKAIHRWL GLTVGVLAVL LGLTGAFLAM DPVQQAWEAP SAPGALPVST LVQRVIHTIP
     AAEEIRRLPS GAIAVFSFAG DQPEASYVNP ADGTVLGAWH ASAVPRWVKN LHRSLLLGDP
     GRWAAAGVAL AMGLLCISAL MLLLRRVGGW RRLTARVRGS LAQRIHVVAG RVVLAVLCLT
     AITALTMSAS TLDLVALDTR IEPEVASLVT GRPDLPGAQL ATLQSLMVKD LRQLNIPGAT
     DPQDTWKVVT TQGRGWIDRY SGQLLAWQDA TVAQRVYDWA LVLHTGEAAW PWAVILGLTG
     ASVLLFWLSG VVIWWQVRSQ APHITGNSPP TQADVLIFVA SEGGSTWGFA QTLHDALRKS
     GHRVYTSPLE DFRTTASARQ VFVLAATYGE GQAPAHASHA LKHIAMLNAG AVPVTVLGFG
     DRLFPSFCAY AEALDQTLRA RGWSSLLPLE RIHQQSGQQF ARWGVALAQA LGEPLVLEHV
     PRVPATVALT LVARQDYPDA FGQAAAILRF SWPIQDLGAR LRGRGLARFA AGDLVGILPP
     GSSVPRYYSL ASGWEDGFLE ICVRHMSGGL CSTHLLGLQA GDCIAAFIRS NSGFALPRSR
     QPVLLIGAGT GVAPLAGFIR RNDRRRPMHL YFGGRDPTRD FYFGPEIQGW LADGRLTTLQ
     TAFSRVPGGG YVQDALRREA ERVRDLIAQG AIVRVCGSRA MAQGVAETLD VVLAPLRLSV
     SALRAKERYA EDVF
//