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Database: UniProt
Entry: A1B7P0_PARDP
LinkDB: A1B7P0_PARDP
Original site: A1B7P0_PARDP 
ID   A1B7P0_PARDP            Unreviewed;       401 AA.
AC   A1B7P0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ABL71534.1};
GN   OrderedLocusNames=Pden_3463 {ECO:0000313|EMBL:ABL71534.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL71534.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) 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; CP000490; ABL71534.1; -; Genomic_DNA.
DR   RefSeq; WP_011749710.1; NC_008687.1.
DR   AlphaFoldDB; A1B7P0; -.
DR   STRING; 318586.Pden_3463; -.
DR   EnsemblBacteria; ABL71534; ABL71534; Pden_3463.
DR   GeneID; 75502861; -.
DR   KEGG; pde:Pden_3463; -.
DR   eggNOG; COG1251; Bacteria.
DR   HOGENOM; CLU_003291_4_0_5; -.
DR   OrthoDB; 7809559at2; -.
DR   Proteomes; UP000000361; Chromosome 2.
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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
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   401 AA;  42491 MW;  B0DAF58378BD4AB8 CRC64;
     MPHVVVIGAG QAGAALAARL RALKFQGEIT VIGDEPAPPY QRPPLSKAYL LGEMEEERLW
     LRSADFWAEN RITLKLGTPV TAIDPVARTV TVGEEVLAYD ELALTTGSVP RRLPAEMGGA
     LGGVHTVRTL ADIDAIRAGF VPGRRLVVIG GGYIGLEAAA VARKLGLEVT VIEMAPRILQ
     RVAAPETALY FRKLHAGHGA AIIEGEGVDR ILGEGRVAGV RLKDGRVLPA DFVIAGVGIV
     PATALAEAAG IALENGIRTD ARGRTSAANV WAAGDCASFP LDGVQIRLES VGNAIDQAEL
     VAANIMGADK DYVPKPWFWS DQYDCKLQIA GLNAGYDRVV ARPGEGEAVS IWYYAGDRLL
     AVDAMNDPRA FMVGKRLIEA GRTADPRLVA DAATDLKALL R
//
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