ID A0A1Q3WNX9_9BACT Unreviewed; 526 AA.
AC A0A1Q3WNX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OJW77100.1};
GN ORFNames=BGO59_23560 {ECO:0000313|EMBL:OJW77100.1};
OS Spirosoma sp. 48-14.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW77100.1, ECO:0000313|Proteomes:UP000186057};
RN [1] {ECO:0000313|EMBL:OJW77100.1, ECO:0000313|Proteomes:UP000186057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=48-14 {ECO:0000313|EMBL:OJW77100.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OJW77100.1}.
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DR EMBL; MKUD01000020; OJW77100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3WNX9; -.
DR STRING; 1895854.BGO59_23560; -.
DR Proteomes; UP000186057; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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 CDD; cd03478; Rieske_AIFL_N; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur 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; IPR028202; Reductase_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 8..103
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 526 AA; 57776 MW; F9B1740CDAC453CF CRC64;
MIADYTEAPV CHVNDLVDGE LKQVRVGDTD VLLARADGQF YALHPQCTHY HGPLVEGVLN
GHRLICPWHN ACFDVRDGHR LEAPALNGLP THEVRIEQDQ VFVRVTTNKE SLENPMATPD
ETNTATYVIV GGGGAAAFAA EAMREGGFTG NIIMLTESDR IPYDRPNCSK EYLQDAAPDE
WMPLRTEEFY TNYGIEIRTG QRVTTLDPIE KRIELASGET LTYDKVLVCP GGQPNTLPGL
NPDLKGVYTL RSLHDSKHLR DLGKQNKRVV IVGSSFIGLE GAMSLRKLGS EVDVVGPEPV
PFRKILGEKI GRVVQGWHEE AGVRFHLGRK VAHLEGDDTV QAVVLDNGER LPADVVLLGL
GVKPRTDFLV GVPLEADGGI STDGNLNSLE GLYAAGDIVH YPTADGSQRI EHWRVACQQG
HVAGLNMAGQ QTPYLSAPFF WTDQQGHQLA YVGHTTAIDD ILYDGDPEKD DSFLALYIQK
NQITAAVGLQ RDQDIIAIRE LMEAGRMPSV DDVRQGIDWV KTLKKA
//