ID A0A0M9ULV2_9MICO Unreviewed; 475 AA.
AC A0A0M9ULV2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=NADPH-dependent mycothiol reductase Mtr {ECO:0000313|EMBL:GAP79683.1};
GN ORFNames=Y09_2534 {ECO:0000313|EMBL:GAP79683.1};
OS Brachybacterium sp. SW0106-09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1704590 {ECO:0000313|EMBL:GAP79683.1, ECO:0000313|Proteomes:UP000037781};
RN [1] {ECO:0000313|EMBL:GAP79683.1, ECO:0000313|Proteomes:UP000037781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW0106-09 {ECO:0000313|EMBL:GAP79683.1,
RC ECO:0000313|Proteomes:UP000037781};
RA Qin Q.L., Li Y., Zhang Y.Z.;
RT "Genome Sequencing of Brachybacterium sp. SW0106-09.";
RL Submitted (SEP-2015) 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:GAP79683.1}.
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DR EMBL; BCAK01000029; GAP79683.1; -; Genomic_DNA.
DR RefSeq; WP_053918003.1; NZ_BCAK01000029.1.
DR AlphaFoldDB; A0A0M9ULV2; -.
DR Proteomes; UP000037781; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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 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}.
FT DOMAIN 34..330
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 360..469
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 459
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 189..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 324
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 475 AA; 51243 MW; 7E2B901CC7F848AD CRC64;
MTETTHYDIA LIGSGSANSF PGPDLADRTI VQIDRGVGPD RVFGGTCLNL GCIPTKMFVH
TADLAATPAD AARFGLTEQL QHVDWPAIRD RIFGRIDPIT AGGEAYRRDH EDNANLTLLR
GTARFVGEKE LLVDGNDGSR QRITADTIVL GAGSRPVLPP IDGLADLAPH TSDTIMRVEA
LPASLAILGS GVVAVEMAHV LSALGVEVTL IARSQRVLRA ADADISARLT ELLGERLHLV
TGFDTTSARR TADGVELRGT REGREETLRA EELLVAVGRR PNSDLLDVRA AGIDVAEDGR
VEVDAYQRVL AGGEVREGVF AFGDLSSPHQ LKHVANHEQR IVRHNVLHPE QLRRSDTMPV
PSGVFTHPHV AWVGMDEETA RASGREVRVA VQEYASIAYG WALEDTTGFA KIIADAETTE
ILGAHLIGPE ATTLIQLLIQ AMSTGQTARD IATTQYWIHP AMPELIENAL LQLVD
//
