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Database: UniProt
Entry: F8DFT0_STREP
LinkDB: F8DFT0_STREP
Original site: F8DFT0_STREP 
ID   F8DFT0_STREP            Unreviewed;       438 AA.
AC   F8DFT0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AEH55291.1};
GN   OrderedLocusNames=HMPREF0833_10260 {ECO:0000313|EMBL:AEH55291.1};
OS   Streptococcus parasanguinis (strain ATCC 15912 / DSM 6778 / CIP 104372 /
OS   LMG 14537).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=760570 {ECO:0000313|EMBL:AEH55291.1, ECO:0000313|Proteomes:UP000001502};
RN   [1] {ECO:0000313|Proteomes:UP000001502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15912 / DSM 6778 / CIP 104372 / LMG 14537
RC   {ECO:0000313|Proteomes:UP000001502};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RT   "Complete sequence of Streptococcus parasanguinis strain ATCC 15912.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR   EMBL; CP002843; AEH55291.1; -; Genomic_DNA.
DR   RefSeq; WP_013903362.1; NC_015678.1.
DR   AlphaFoldDB; F8DFT0; -.
DR   GeneID; 75175171; -.
DR   KEGG; scp:HMPREF0833_10260; -.
DR   HOGENOM; CLU_016755_1_2_9; -.
DR   Proteomes; UP000001502; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DOMAIN          4..301
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          328..434
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        425
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         164..171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         250
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         291
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   438 AA;  47155 MW;  53AA3D89A90D05BD CRC64;
     MLMYDVIVIG FGKAGKTLAA KLSSQGKKVA LIEKSKSMYG GTCINIACIP TKTLIVAAEK
     GLDFEQAMNE KNAVITRLNG KNYATIAGTG VDIIDATARF LSNKVIEIQA GDEKEELTAE
     TIIINTGAVP TILPIPGLAE SKFAVDSTGI QRLENLPKRL GVLGGGPIGL EFAHLYNTLG
     SQVTVLDASE TFLPRIEPSI AALAKSYLEE DGIQFLQGVH TQEIKDDQNS LTVVTDKGDF
     EFDILLYATG RKPNTAGLGL ENTDIQVTDR GAIQVNRHLE TSVPGVFAVG DVNGGPQFTY
     MSLDDFRIVF NYLTGDGSYN LETRRNYATT LFIAPPLAQV GLTEQEARDK GLPVAVKELP
     VAAMPRGHVN ADLRGAFKAV VNPETKEILG ATLFGEAAGE LINLITMAMD NKIPYTYIAK
     QIFTHPTMAE NLNDLFAI
//
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