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Database: UniProt
Entry: I1X5F0_9BACT
LinkDB: I1X5F0_9BACT
Original site: I1X5F0_9BACT 
ID   I1X5F0_9BACT            Unreviewed;       429 AA.
AC   I1X5F0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sulfur/thiosulfate oxidation protein SoxF {ECO:0000313|EMBL:AFI78725.1};
GN   Name=soxF {ECO:0000313|EMBL:AFI78725.1};
GN   ORFNames=ws406H10_0013 {ECO:0000313|EMBL:AFI78725.1};
OS   uncultured bacterium ws406H10.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=1131831 {ECO:0000313|EMBL:AFI78725.1};
RN   [1] {ECO:0000313|EMBL:AFI78725.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22739490; DOI=10.1038/ismej.2012.66;
RA   Lenk S., Moraru C., Hahnke S., Arnds J., Richter M., Kube M., Reinhardt R.,
RA   Brinkhoff T., Harder J., Amann R., Mussmann M.;
RT   "Roseobacter clade bacteria are abundant in coastal sediments and encode a
RT   novel combination of sulfur oxidation genes.";
RL   ISME J. 6:2178-2187(2012).
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DR   EMBL; JQ256789; AFI78725.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1X5F0; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.90.760.10; Flavocytochrome c sulphide dehydrogenase, flavin-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR049386; FCSD_central.
DR   InterPro; IPR015323; FlavoCytC_S_DH_flav-bd.
DR   InterPro; IPR037092; FlavoCytC_S_DH_flav-bd_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43755; -; 1.
DR   PANTHER; PTHR43755:SF1; POSSIBLE DEHYDROGENASE_REDUCTASE; 1.
DR   Pfam; PF09242; FCSD-flav_bind; 1.
DR   Pfam; PF21706; FCSD_central; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
FT   DOMAIN          40..169
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          173..287
FT                   /note="Sulfide dehydrogenase [flavocytochrome c]
FT                   flavoprotein chain central"
FT                   /evidence="ECO:0000259|Pfam:PF21706"
FT   DOMAIN          363..428
FT                   /note="Flavocytochrome c sulphide dehydrogenase flavin-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF09242"
SQ   SEQUENCE   429 AA;  45755 MW;  D5996E2189BDB2D1 CRC64;
     MSKPREETMK LNRRLFLSAT GAGAATLAMP SLSLGQAKPK VVVIGGGAGG ATAARYIAKD
     SKGEIAVTLI EASKRYYTCF FSNLYLGGFR DYASIGHGYD ALAADHGVNV VHDWAASVDA
     GTKQVRLASG ASISYDRLVL SPGIDMKYDS VPGYSAEAQG RMPHAWKSGT QVQQLRSQVE
     NMREGGTFVM VPPPNPFRCP PGPYERISMI AHILKQKNPS AKIIVVDPKP KFSKQALFQE
     GWEAHYPDMI EWLGPDIHGG IKNVNTDTME IETDLETFKA DAASVVPAQK AGSIAMAAGV
     TDGDWAPIVP TSMQSKADPN IYVLGDASIA AAMPKSGFSA NSQAKVAANA IRGELTGSKV
     FPARYANTCW SLIATDDGVK VGANYGAGAD KIEVVDKFIS KTGEDEAVRK ATYEESEGWY
     KGITADIFG
//
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