ID G0L4N8_ZOBGA Unreviewed; 418 AA.
AC G0L4N8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:CAZ98810.1};
DE EC=1.18.1.- {ECO:0000313|EMBL:CAZ98810.1};
GN OrderedLocusNames=zobellia_4675 {ECO:0000313|EMBL:CAZ98810.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ98810.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ98810.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FP476056; CAZ98810.1; -; Genomic_DNA.
DR RefSeq; WP_013995997.1; NC_015844.1.
DR AlphaFoldDB; G0L4N8; -.
DR SMR; G0L4N8; -.
DR STRING; 63186.ZOBELLIA_4675; -.
DR KEGG; zga:ZOBELLIA_4675; -.
DR PATRIC; fig|63186.3.peg.4583; -.
DR HOGENOM; CLU_003291_4_0_10; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CAZ98810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898}.
FT DOMAIN 10..310
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 329..411
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 418 AA; 45487 MW; 17A36F4C291FC4E6 CRC64;
MSDIPNNEPS CVVIGASHAG VNFAFALRRE GWNGSICLID ADSVLPYHRP PLSKAYLTSD
DGIEKNLLKS KESYVKERIE LKLGVWVDAI DRESKTIILA DGTTVAYDKL VLATGARPIM
PPIPGLDTAK NLFPLRSAAD VANIKKTVAE NESLQVVVIG GGYIGLETAA SLKKLGASVT
VLERESRILA RVTAPEMSAF FQKLHRDNHV SVLTEKNVTS IEPTSNGNTV VCSDGSSYPA
DMVIVGVGIH VNKELAEKAG LTIENGIRVN EMAQTSDASI YAIGDCTFHY NPHYDRYIRL
ESVQNAVDQA KIAAAAIAGK KCCYDTLPWF WSDQYDVKLQ MVGLSDGYDE VVVREEADKP
NCFSVWYFKG DTLLSVDAVN NAKAYVYGTK FIKGGEKIDK SKLGDPTAEF KPANLVAQ
//
