ID C3K988_PSEFS Unreviewed; 401 AA.
AC C3K988;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Dioxygenase system reductase component {ECO:0000313|EMBL:CAI2796639.1, ECO:0000313|EMBL:CAY48624.1};
GN OrderedLocusNames=PFLU_2392 {ECO:0000313|EMBL:CAY48624.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY48624.1};
RN [1] {ECO:0000313|EMBL:CAY48624.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY48624.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2796639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2796639.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; OV986001; CAI2796639.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY48624.1; -; Genomic_DNA.
DR AlphaFoldDB; C3K988; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_6; -.
DR Proteomes; UP001152918; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:CAY48624.1};
KW Oxidoreductase {ECO:0000313|EMBL:CAY48624.1}.
FT DOMAIN 7..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 314..399
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 401 AA; 42721 MW; 88E9F4BE48F8C153 CRC64;
MTMSAPLIIV GAGHAGGRAA LTLREEGYTG RLILIGDEPH LPYERPPLSK AVLQGTADLA
GCSLCDSARL TELGIEHIAG HPVTQLEPEH HRLQLADGQW LPYAGLLLAT GGRARRLPQE
QAHVLYLRTH DEALALRNAL KAGTRLVVVG GGFIGLEVAA TARGLGCEVT LLEAGPRLAG
RVLPPVISEA LLALHRQHGV DVRLNVALES IQADAVLLVD GQRLPCDLVV VGIGMQPNIE
LATAAGLDVG QGIRVDTHLR TSAPDIYAAG DVCEFRLGGL YQRQETWRNA EVQGRHAALN
LLGHDVPFDA LPGFWSDQYD WGLQTVGVIT PLTVSRPLAG GGVLLFYLDA EHHLHGACGW
APGNSVAKDI KLCERLISAR IPLNAASLAD PELSLKHLLR G
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