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Database: UniProt
Entry: A0A1G9SCC3_9FLAO
LinkDB: A0A1G9SCC3_9FLAO
Original site: A0A1G9SCC3_9FLAO 
ID   A0A1G9SCC3_9FLAO        Unreviewed;       734 AA.
AC   A0A1G9SCC3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Sulfite reductase (NADPH) flavoprotein alpha-component {ECO:0000313|EMBL:SDM33042.1};
GN   ORFNames=SAMN04488514_107218 {ECO:0000313|EMBL:SDM33042.1};
OS   Kriegella aquimaris.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kriegella.
OX   NCBI_TaxID=192904 {ECO:0000313|EMBL:SDM33042.1, ECO:0000313|Proteomes:UP000199440};
RN   [1] {ECO:0000313|EMBL:SDM33042.1, ECO:0000313|Proteomes:UP000199440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19886 {ECO:0000313|EMBL:SDM33042.1,
RC   ECO:0000313|Proteomes:UP000199440};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNGV01000007; SDM33042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9SCC3; -.
DR   STRING; 192904.SAMN04488514_107218; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000199440; 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   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 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:SF84; METHIONINE SYNTHASE 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:UP000199440};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..480
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          495..595
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   734 AA;  82463 MW;  497D9CE162F0BF09 CRC64;
     MTLSIWRYSH LILAVSSSLF LLVASITGVI LSVEPINNKL QPYSISNAEG LSLAETLANI
     NARYDDVISV SQDQNGFVSA TVIIDSKNES FYIDPITGDK LGPIIEKAPI YQFATNLHRS
     LFLKTPGRLF IGLASLLLFF IAVSGIVLIA KRQGGIQRFF SSVVRENYAQ YQHVVYSRIV
     LIPIVILALS GVYLSLLRFQ LIPETFITHE IDFDNLQEEP LLDYTNFELL KNTPLSELRD
     IEYPFSEFVE DYYLIRLKNK EVLLNQYTGA PISEKKYPMV TLASEWATVL HTGQGTILWS
     IVLGLGSLAV PFLMFTGFAV YFKRPKTNIK NTVPKEKARF VILVGSEGGT TLQYAQLLHS
     QLLALGKKSY LAMMDDYTTF KSMEHLVVIT ATYGQGEAPS SAIKFETLLK KHIQKQPYHF
     SVVGFGSTSY PHFCEFAYET NKLLQTTPKA NALIAQVHTV NDRSFEAYTN WATAWGNLVG
     LNIRLTKPTK LAEKSHKSPF IVLEKTEAQD MIDDTFLLTL KNTNGAQANS GDLLSIVPGS
     GEQERLYSLG KLDDNIFTIS VKRHPEGLCS NYLLQLEKGT TFSASVVANK NFHFPKKAKK
     TVLIATGTGI GPFLGMIRSN SRKNEIHLYW GGRTEDSLKL YKPFIDNALE SGSLTTFIPA
     YSRTQTEKKY VQHLIKQDGE QIAKVLRKKG CVMICGSIAM QKEVLNELQS ICNRYLKKDL
     SFYQNRKQIK MDCY
//
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