ID A0A1R1L9T7_9MICC Unreviewed; 476 AA.
AC A0A1R1L9T7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Mycothione reductase {ECO:0000313|EMBL:OMH24251.1};
GN ORFNames=BKD30_08905 {ECO:0000313|EMBL:OMH24251.1};
OS Tersicoccus phoenicis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Tersicoccus.
OX NCBI_TaxID=554083 {ECO:0000313|EMBL:OMH24251.1, ECO:0000313|Proteomes:UP000187085};
RN [1] {ECO:0000313|EMBL:OMH24251.1, ECO:0000313|Proteomes:UP000187085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1p05MA {ECO:0000313|EMBL:OMH24251.1,
RC ECO:0000313|Proteomes:UP000187085};
RA Nakajima Y., Yoshizawa S., Nakamura K., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Tersicoccus phoenicis 1P05MA.";
RL Submitted (DEC-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:OMH24251.1}.
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DR EMBL; MRDE01000063; OMH24251.1; -; Genomic_DNA.
DR RefSeq; WP_076704091.1; NZ_MRDE01000063.1.
DR AlphaFoldDB; A0A1R1L9T7; -.
DR STRING; 554083.BKD30_08905; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000187085; 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; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW NAD {ECO:0000256|ARBA:ARBA00023027, 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:UP000187085}.
FT DOMAIN 6..334
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 355..468
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 49
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 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 40..45
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 476 AA; 50897 MW; E97C90CC5C37D8E0 CRC64;
MSSHHDLVIV GSGSGNSILG PEWDGRSVAI VEGGTFGGTC LNVGCIPTKM FVYPAGLAAV
PAEAARLGVD LTRDAVHWQR IRDRIFGRVD AISANGRAYR DVEQKNVTLY GEHARMTGPR
ELVTDSGRTV TADAVVIAAG SRPRELPVPG AALPQVHSSD TIMRIPHPPR RLVIVGGGYV
AAEFAAIFHQ IGVAVTQVVR GTTLLRDLDE TIADRFTRAA RDQWDVRLGT EITAIAPIDE
EHPGTGPVRV SLMDAEDRDA GHVDADLVLI AVGRIPNTDR LGAGAVGLDL HHDGRLRVDQ
FQRVLAAGRP APGVWALGDI CSEYQLKHVA NHEARVVAHN LTTTGSLLAS DHRFVPSAVF
THPQLAQVGM TEAQARSHCA AVGQDLAVAV QDYGSTAYGW AMEDRTGIVK LLAERGTGRI
LGAHLLGHEA SMLIQPLVQA MHTGLPAHRM ARGQYWIHPA LTEVVENALL NLHTGA
//
