ID A0A1A3MZ95_MYCAS Unreviewed; 474 AA.
AC A0A1A3MZ95;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=NAD(P)H-quinone dehydrogenase {ECO:0000313|EMBL:OBK14405.1};
GN ORFNames=A5636_08575 {ECO:0000313|EMBL:OBK14405.1};
OS Mycobacterium asiaticum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1790 {ECO:0000313|EMBL:OBK14405.1, ECO:0000313|Proteomes:UP000093629};
RN [1] {ECO:0000313|EMBL:OBK14405.1, ECO:0000313|Proteomes:UP000093629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245139.5 {ECO:0000313|EMBL:OBK14405.1,
RC ECO:0000313|Proteomes:UP000093629};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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:OBK14405.1}.
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DR EMBL; LZLQ01000098; OBK14405.1; -; Genomic_DNA.
DR RefSeq; WP_065159567.1; NZ_LZLQ01000098.1.
DR AlphaFoldDB; A0A1A3MZ95; -.
DR OMA; GCEVASM; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000093629; Unassembled WGS sequence.
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:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 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:UP000093629}.
FT DOMAIN 4..335
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 355..464
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 192..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 474 AA; 49466 MW; 0106086526D225F5 CRC64;
MVTRIVILGG GPAGYEAALV AAARGPEIAQ VTVVDADGIG GAAVLCDCVP SKTFIASTGL
RSELRRASPG LNIDMAEAIS LPGIHQRVKT LAAAQSADIT ADLLSMGVEL IAGHGELVDA
TPGLARHCVK VTHSDPGREG PITSTHDADV VLIATGASPR ILPSAQPDDQ RILTWRQLYD
LDVLPEHLIV VGSGVTGAEF VNAYTELGVT VTVVASRDRV LPYEDADAAL VLEESFAERG
VKLVKNARAQ SVTRSADGVV VAMTDGRTVT GSHALMTIGS IPNTGGLGLE RVGIELDRGN
YLTVDRVSRT SVPGVYAAGD CTGLLPLASV AAMQGRIAMY HALGEAVHPI RLRTVAATVF
TRPEIAAVGV PQKEIDDGSV RARTIMLPLE TNARAKMSGL RHGFVKLFCQ QATGVVIGGV
VVAPIASELI LPIAMAVQNR ITVNELAETL AIYPSLSGSI TEAARRLIAH HDLD
//