ID E3HCK4_ILYPC Unreviewed; 280 AA.
AC E3HCK4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Sulfite reductase, subunit B {ECO:0000313|EMBL:ADO83980.1};
GN OrderedLocusNames=Ilyop_2217 {ECO:0000313|EMBL:ADO83980.1};
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OG Plasmid pILYOP01 {ECO:0000313|EMBL:ADO83980.1,
OG ECO:0000313|Proteomes:UP000006875}.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO83980.1, ECO:0000313|Proteomes:UP000006875};
RN [1] {ECO:0000313|EMBL:ADO83980.1, ECO:0000313|Proteomes:UP000006875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC {ECO:0000313|Proteomes:UP000006875};
RC PLASMID=pILYOP01 {ECO:0000313|Proteomes:UP000006875};
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR006816-1};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR006816-2};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002282; ADO83980.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HCK4; -.
DR KEGG; ipo:Ilyop_2217; -.
DR HOGENOM; CLU_003827_1_1_0; -.
DR Proteomes; UP000006875; Plasmid pILYOP01.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd06221; sulfite_reductase_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR014260; Sulphite_reductase_B.
DR NCBIfam; TIGR02911; sulfite_red_B; 1.
DR PANTHER; PTHR43513:SF1; ANAEROBIC SULFITE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW Plasmid {ECO:0000313|EMBL:ADO83980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006875}.
FT DOMAIN 18..111
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 79..81
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 248
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 253
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 256
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 264
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 280 AA; 31834 MW; A3A8321A6CBDE02F CRC64;
MNNTYIPGNP YTPIENVYLP KGYKLISLNK LTEIEWLFRV EYDQEVTFGQ FIEISIPRVG
EAPLSVTQFN KEEGWIEFLI RKVGKVTDCL FDLKAGDLMF LRGPYGNGFP AEEEYRGKHL
IIVAGGSGLA PVRSMINHFY NDEANDTKVD LLLGFKDYDS IIFKDEIKQW KEKFNTLITV
DNSCSIDGVC EGLVTKYIPD LELADDIADM EVVIVGPPVM MKYSALEFLS RGVPKEKIWV
SFERKMSCGV GKCGHCKIDE TYICLEGPVF RYDEAEKLVD
//
