ID Q3SIV0_THIDA Unreviewed; 473 AA.
AC Q3SIV0;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Putative pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AAZ97425.1};
GN OrderedLocusNames=Tbd_1472 {ECO:0000313|EMBL:AAZ97425.1};
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ97425.1, ECO:0000313|Proteomes:UP000008291};
RN [1] {ECO:0000313|EMBL:AAZ97425.1, ECO:0000313|Proteomes:UP000008291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ97425.1,
RC ECO:0000313|Proteomes:UP000008291};
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97425.1; -; Genomic_DNA.
DR RefSeq; WP_011311984.1; NC_007404.1.
DR AlphaFoldDB; Q3SIV0; -.
DR STRING; 292415.Tbd_1472; -.
DR KEGG; tbd:Tbd_1472; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_2_4; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000008291; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008291}.
FT DOMAIN 11..336
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 356..462
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 186..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 321
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 47..52
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 473 AA; 50143 MW; B6E4D22187BC4929 CRC64;
MGSETDHDNF DAVIVGAGQA AAPLAVALGA AGWRTAVVER RHVGGSCINF GCTPTKAMAA
SARVAALARR AAEFGLRAGT VEVDFPAVMQ RARAIVARFR RRLEASLAGA DNVELIFGDA
IFQDARTLIV RRPDGESRTL AAAHVFINTG TRAALPPIPG LERLPLLHDD ALLALETLPP
HLLVIGGGYV GLEFAQMFRR FGSEVSLIQR DEQLAPREDP DVAEALREML VEDGVKVYLE
AKILDADRGR SSDGDSIALN LKTPTGPLRL LGSHLLVATG RRPNSDDLDL AAAGVETGAD
GYIRVNDRLE TSAAGIYALG DVKGGPAFTH IAYDDARVLK TNLLGDGGAS VADRPVPYTV
FTDPQLGRIG LSEREARQSG RRVLRAHLQM AQVARAIETG EARGFVKALI DADSGEILGA
AALGADGGEL MAMLQLAMMG RIPYSRLHDA VFAHPTLAES LNALFAAPQP LPR
//
