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Database: UniProt
Entry: A0A5S5DUB6_9FLAO
LinkDB: A0A5S5DUB6_9FLAO
Original site: A0A5S5DUB6_9FLAO 
ID   A0A5S5DUB6_9FLAO        Unreviewed;       700 AA.
AC   A0A5S5DUB6;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   SubName: Full=Sulfite reductase (Ferredoxin) {ECO:0000313|EMBL:TYP99477.1};
GN   ORFNames=C7447_10175 {ECO:0000313|EMBL:TYP99477.1};
OS   Tenacibaculum adriaticum.
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=413713 {ECO:0000313|EMBL:TYP99477.1, ECO:0000313|Proteomes:UP000323136};
RN   [1] {ECO:0000313|EMBL:TYP99477.1, ECO:0000313|Proteomes:UP000323136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18961 {ECO:0000313|EMBL:TYP99477.1,
RC   ECO:0000313|Proteomes:UP000323136};
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 (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:TYP99477.1}.
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DR   EMBL; VNIA01000001; TYP99477.1; -; Genomic_DNA.
DR   RefSeq; WP_148868199.1; NZ_VNIA01000001.1.
DR   AlphaFoldDB; A0A5S5DUB6; -.
DR   OrthoDB; 9803707at2; -.
DR   Proteomes; UP000323136; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein,Domain 2; 1.
DR   InterPro; IPR051329; NIR_SIR_4Fe-4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   PANTHER; PTHR32439:SF9; BLR3264 PROTEIN; 1.
DR   PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000323136}.
FT   DOMAIN          47..113
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          122..276
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          323..389
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          398..536
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   700 AA;  79625 MW;  105854EC122021AD CRC64;
     MQSFRSEIEN PIVEKDILEL ERKIQLFKEG KIDEERFRSL RLARGVYGQR QLGVQMIRIK
     LPYGKVSSEQ LHRIANVSDE YSRGRLHITT RQDIQIHHVS LDRTPELWAQ LEKDDITLRE
     ACGNAVRNVT ASETAGIDIN EPFDVSPYAH ATFQFFLRNP ICQEMGRKFK MSFSATDDDT
     ALSFMHDLGF IAKTKTINKK EVKGFKVLLA GGLGSQPRHA DVIYEFLEAD LLIPTIEGVL
     RVFDRYGERS KRAKARLKFL VKDLGVNEFL TLIETERKAL AYQSYPIDTS KFEEEPVFKT
     NDIPSVTILN QKAYQEWKET NVIKQKQEGL YAIGIKVHLG DFYTDKARLL ADLIKKYAAN
     ELRFTLRQNI LIRHVREAFL PFFYTELQKL GFAEIGYNSL SDITACPGTD TCNLGISSST
     GIAAELERVL KTEYPKYSNN KDITIKISGC MNACGQHNMA HIGFQGMSIK VGNLLAPALQ
     VLIGGGILGN GKGRFSDKLI KIPSKKGPEA LRILLNDFEK NQKIKEPYLD YYDRLGKTYF
     YDLLKHLSDI TNLKEDDFID WGHDQNYIKA IGVGECAGVV IDLIATLLFE SEEKLDNATE
     ACNEKQWSNS IYFSYTAIIN TAKALLTAEE EKTNTQAGII TNFDTVFVAT KKIDLPVSFS
     DFVYQINKNE PTETFAKKYL QEAKDFYKTI DAYRKATIEK
//
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