ID A0A0N1MSP1_9SPHN Unreviewed; 408 AA.
AC A0A0N1MSP1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=3-phenylpropionate/trans-cinnamate dioxygenase ferredoxin reductase subunit {ECO:0000313|EMBL:TCM37626.1};
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KPH59260.1};
GN ORFNames=ADT71_24380 {ECO:0000313|EMBL:KPH59260.1}, EDF59_11021
GN {ECO:0000313|EMBL:TCM37626.1};
OS Novosphingobium sp. ST904.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH59260.1, ECO:0000313|Proteomes:UP000037878};
RN [1] {ECO:0000313|EMBL:KPH59260.1, ECO:0000313|Proteomes:UP000037878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:KPH59260.1,
RC ECO:0000313|Proteomes:UP000037878};
RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA Vangronsveld J.;
RT "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT stimulates plant growth.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TCM37626.1, ECO:0000313|Proteomes:UP000295740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:TCM37626.1,
RC ECO:0000313|Proteomes:UP000295740};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (MAR-2019) 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:KPH59260.1}.
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; LGJH01000162; KPH59260.1; -; Genomic_DNA.
DR EMBL; SLVC01000010; TCM37626.1; -; Genomic_DNA.
DR RefSeq; WP_054441140.1; NZ_SLVC01000010.1.
DR AlphaFoldDB; A0A0N1MSP1; -.
DR STRING; 1684385.ADT71_24380; -.
DR PATRIC; fig|1684385.3.peg.5087; -.
DR OrthoDB; 7809559at2; -.
DR Proteomes; UP000037878; Unassembled WGS sequence.
DR Proteomes; UP000295740; Unassembled WGS sequence.
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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:TCM37626.1};
KW Oxidoreductase {ECO:0000313|EMBL:TCM37626.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037878}.
FT DOMAIN 5..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 324..408
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 408 AA; 43534 MW; DDB51C797E911A9F CRC64;
MSKADVVIVG AGHGGAQCAI ALRQNGFEGT ITVIGREPEH PYERPPLSKE YFAREKTFDR
LYIRPPTFWA EKEITFKLGT EVTKVDAAAR ELTLSNGETY GYGKLVWATG GDPRRLSCSG
ADLAGVHAVR TREDCDTLMA EVDAGTKNVV VIGGGYIGLE AAAVLSKMGL SVTLLEALPR
VLARVAGEPL SEFYQKEHRD HGVDLRTGVA VECLVGDGHK VTGVQLADGA VLPAEAVIVG
IGIVPAVGPL ILAGAAGANG VDVDEYCRTS LPDIYAIGDC AAFACDFAGG AVMRVESVQN
ANDMATCVAK AICGDEKPYK AFPWFWSNQY DLRLQTAGIN LGFDQTVIRG NPEDRSFSVV
YLKEGKVLAL DCVNMVKDYV QGRKLVEAGA KPDLAALADK EKPLKELL
//