ID D5XFN4_MYCMR Unreviewed; 450 AA.
AC D5XFN4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:CAM96529.1};
GN Name=pMM23-09 {ECO:0000313|EMBL:CAM96529.1};
OS Mycobacterium marinum.
OG Plasmid pMM23 {ECO:0000313|EMBL:CAM96529.1}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=1781 {ECO:0000313|EMBL:CAM96529.1};
RN [1] {ECO:0000313|EMBL:CAM96529.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-535 {ECO:0000313|EMBL:CAM96529.1};
RC PLASMID=pMM23 {ECO:0000313|EMBL:CAM96529.1};
RA Schue M., Dover L.G., Besra G.S., Parkhill J., Brown N.L.;
RT "A novel plasmid-encoded mercury resistance operon from Mycobacterium
RT marinum : sequence, functional characterisation and potential use as a non-
RT antibiotic resistance cassette in mycobacteria.";
RL Mol. Microbiol. 0:0-0(2007).
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; CU462862; CAM96529.1; -; Genomic_DNA.
DR AlphaFoldDB; D5XFN4; -.
DR OMA; VGGCDNT; -.
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 Plasmid {ECO:0000313|EMBL:CAM96529.1}.
FT DOMAIN 5..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..444
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 173..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 450 AA; 47928 MW; 2B244BF7923FF8B8 CRC64;
MTARFDVIVI GAGMAGIAAA NKCGAQGWRV AIVDSLPYGG TCALRGCDPK KILRRGAEII
DASRLMRGKG IDEGQIRINW TDLMRHKRGF TDPAPANMEN DLRRHGVQTL HGQARFVDAH
QISVGDDVHH TERFLVATGA RPRPLQFDGH EHLIDSTQFL DLEDLPPRIV FVGGGYISFE
FAHIAARAGS HPIILDHGPR PLKGFDPDLV DLLIGRGVAA GVDVRASTTV TAVRATATGY
QVQVNQDGTD ATIDADVVVH GAGRLPELAD LDLDRAGIAW SERGIRVQPH LQSTTQPGVY
AAGDAADTAG PPLTPVAVIE GKVAASNMLK AASTVPDYTG IPSAVFTIPE LARVGLLEAE
ARDQGLNIDV RYSDASTWYS SYRIGEGTAA AKILVNKDDD RIVGAHLLGP DYTEHANTIA
VAIKLGLTTR QLKTTTAAYP TLGSDLGSML
//
