ID A0A345QSL6_9RHOB Unreviewed; 402 AA.
AC A0A345QSL6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AXI48303.1};
GN ORFNames=C1J03_21295 {ECO:0000313|EMBL:AXI48303.1};
OS Sulfitobacter sp. SK012.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389005 {ECO:0000313|EMBL:AXI48303.1, ECO:0000313|Proteomes:UP000253903};
RN [1] {ECO:0000313|EMBL:AXI48303.1, ECO:0000313|Proteomes:UP000253903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK012 {ECO:0000313|EMBL:AXI48303.1,
RC ECO:0000313|Proteomes:UP000253903};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP025804; AXI48303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345QSL6; -.
DR KEGG; sulz:C1J03_21295; -.
DR OrthoDB; 7809559at2; -.
DR Proteomes; UP000253903; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 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 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 PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000253903}.
FT DOMAIN 3..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 317..400
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 402 AA; 43369 MW; 65F8764F62A06D08 CRC64;
MRHIVVVGAG QAGSSCVAKL RNDGFDGKVT LIGAEPVPPY QRPPLSKAYL LGDMALERLY
LRPESFYSEH DIDLRMGRPV SHLDIDARKI SISSETFEYD ELVLTTGSVP NRLPGAIGGA
LEGVHVVRDL SDVDAMSPRF IKGTRVLIVG GGYIGLEAAA VASKLGLKVT LVEQSERILQ
RVAAPETSDF FRDLHTKHGV DIREGVGLDH LQGEVNVTGA MLNDHSELAV DFVIAGVGIR
PGTGLAETAG IEIKNGIKVD AHGRTSAPHV WAAGDCTSFP YRGGRIRLES VPNAIEQAEV
VAANLMGAGK EYVAAPWFWS DQYDVKLQIA GLNTGYDRVI TRRTDADSLS IWYYRGDDLL
AVDAMNDPRG FMVGKRLIEG GKSPDPTAIM DPSTDLKALL RA
//
