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Database: UniProt
Entry: A0A0A0F318_9GAMM
LinkDB: A0A0A0F318_9GAMM
Original site: A0A0A0F318_9GAMM 
ID   A0A0A0F318_9GAMM        Unreviewed;       846 AA.
AC   A0A0A0F318;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Sulfite reductase subunit alpha {ECO:0008006|Google:ProtNLM};
GN   ORFNames=N799_01780 {ECO:0000313|EMBL:KGM56910.1};
OS   Lysobacter arseniciresistens ZS79.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM56910.1, ECO:0000313|Proteomes:UP000029989};
RN   [1] {ECO:0000313|EMBL:KGM56910.1, ECO:0000313|Proteomes:UP000029989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS79 {ECO:0000313|EMBL:KGM56910.1,
RC   ECO:0000313|Proteomes:UP000029989};
RX   PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA   Liu L., Zhang S., Luo M., Wang G.;
RT   "Genomic information of the arsenic-resistant bacterium Lysobacter
RT   arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT   genomes.";
RL   Stand. Genomic Sci. 10:88-88(2015).
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:KGM56910.1}.
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DR   EMBL; AVPT01000007; KGM56910.1; -; Genomic_DNA.
DR   RefSeq; WP_036209211.1; NZ_AVPT01000007.1.
DR   AlphaFoldDB; A0A0A0F318; -.
DR   STRING; 913325.N799_01780; -.
DR   eggNOG; COG0369; Bacteria.
DR   eggNOG; COG3182; Bacteria.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000029989; 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; cd06200; SiR_like1; 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   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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR005625; PepSY-ass_TM.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR34219:SF3; BLL7967 PROTEIN; 1.
DR   PANTHER; PTHR34219; IRON-REGULATED INNER MEMBRANE PROTEIN-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          391..528
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          542..708
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   846 AA;  91777 MW;  9443A44E99C4CC9E CRC64;
     MTTTFRNVIF QVHWFLGITA GVVLALVGVT GGILSFEDEL LEALNPGVMT VEPAGRTPLS
     PATLVERVGA ARPGEAIASL ELSSGPRDAA VVGFAPKDGE RRGARRHVDP YSGEVLPEPR
     YRGFFRTTMQ LHRWLAADDV GKQIVGASTV ILVFFCVSGL YLRWPRRWGS LRSWLALDWK
     QKGRNFLWHL HSIVGTWVLV AYLVMSLTGL WWSYGWYRDA VNAWAASGTP ERVEAAAPAD
     RGAPPALDID AAWQAFVASA PAWSSATLSL PRDDGPLSFR YLDADPAHER ARNSLDLDRW
     TLQPVGHERY DDRSLRQKIG GSMFPLHRGS FFGTTGVVVF MLASLLMPLF AVTGWMLYLD
     RRRRKRATMT AAAALAAQPP APAQGPSSDP ILVLHASQTG TAEQIALRTA ATLRDGGCAV
     EVQPLGAVTP AALAGRQVLF VAATFGEGEP PDGARAFTRK LRDGAVSLAG LRYGVLALGD
     RGYRDSYCAF GRELDQHLHH AGAQPLFDRV EVDDGDPAAL RHWQHHLGQI SGNTDAPDWR
     APDYRRWELV ERRLLNPGSA GGPAFHLALQ PGDAADLQWQ AGDIAEIGPR HPAARIDAWL
     AAAGLRGDTP VGIAGNEEPL SAALARSQLP MPQPGTTAQA VADALQPLPH REYSIASLPA
     DGSLQLLVRR MDRPDGQAGL GSGWLTGDAA IGQAIDLRIR SNPGFHPPAD DRPLLLVGNG
     TGLAGLRALL KARIAAGHSR NWLVFGERNA AHDAFHNDEL EAWQRDGQVR LDRVYSRDQP
     ERHYVQHRLA ESADEIREWV EAGASIHVCG SLEGMAPGVD AALAAILGTD RLEAMAAEGR
     YRRDVY
//
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