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Database: UniProt
Entry: A0A1Y2MZ44_PSEAH
LinkDB: A0A1Y2MZ44_PSEAH
Original site: A0A1Y2MZ44_PSEAH 
ID   A0A1Y2MZ44_PSEAH        Unreviewed;       452 AA.
AC   A0A1Y2MZ44;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Mycothione reductase {ECO:0000313|EMBL:OSY40107.1};
DE            EC=1.8.1.15 {ECO:0000313|EMBL:OSY40107.1};
GN   Name=mtr_2 {ECO:0000313|EMBL:OSY40107.1};
GN   ORFNames=BG845_02930 {ECO:0000313|EMBL:OSY40107.1};
OS   Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS   autotrophica).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY40107.1, ECO:0000313|Proteomes:UP000194360};
RN   [1] {ECO:0000313|EMBL:OSY40107.1, ECO:0000313|Proteomes:UP000194360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 535 {ECO:0000313|EMBL:OSY40107.1,
RC   ECO:0000313|Proteomes:UP000194360};
RA   Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT   "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT   potential of specific P450 cytochromes.";
RL   Submitted (SEP-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       ECO:0000256|RuleBase:RU003691}.
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:OSY40107.1}.
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DR   EMBL; MIGB01000014; OSY40107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2MZ44; -.
DR   STRING; 2074.BG845_02930; -.
DR   OrthoDB; 4678789at2; -.
DR   Proteomes; UP000194360; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050627; F:mycothione reductase activity; IEA:UniProtKB-EC.
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   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
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.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194360}.
FT   DOMAIN          5..310
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          339..447
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        437
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         176..183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         262
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        39..44
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   452 AA;  48286 MW;  2CC5D1E9614EC4AB CRC64;
     MAHHDLAVVG TGSGNTIVDE RFAGLDVVHV EATRFGGTCL NVGCIPTKML AHTAEIAESV
     RTASRLGIDA RIDRIRWRDI VDRVYGRLDP IGDDGREYRS EHGTVHIGHA RFTGPRAMTV
     ELAEGGTTAF TADRIVLATG GRPVVPPPVA DSGVPFDTSD TIMRIGELPR HLAVLGGGYI
     AAELAHVFGG LGCEVTIVEL ADTLLDGMDE TVTERFTAAA RERFDVRTGR SVERVTGSAG
     DVRLHLDDGT QVRADRLLVA AGRIPNGDRM DLAAGGVATH DDGRVRVDRH GRTTADGVWA
     LGDVSTPHPL KHVANHEATI VAHNLAHPDD LRTVDHDRVP AAVFASPQVG TVGRTGQQCR
     AEGLAHRTGL HEYGDVAYGW AMEEQRGFCK IITSPDGTLL GAHVLGPQAS VLVQQLVQAM
     ALGTTAQQLA DVQYWIHPAL SEVVENALRD AQ
//
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