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
//