ID A0A0B2AAH8_9MICO Unreviewed; 406 AA.
AC A0A0B2AAH8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KHK98621.1};
GN ORFNames=LK09_06630 {ECO:0000313|EMBL:KHK98621.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK98621.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK98621.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK98621.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KHK98621.1}.
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DR EMBL; JTDK01000006; KHK98621.1; -; Genomic_DNA.
DR RefSeq; WP_039397309.1; NZ_JTDK01000006.1.
DR AlphaFoldDB; A0A0B2AAH8; -.
DR STRING; 1348253.LK09_06630; -.
DR OrthoDB; 1145at2; -.
DR Proteomes; UP000031030; 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; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000031030}.
FT DOMAIN 3..300
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 319..405
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 406 AA; 42893 MW; B7C55E5AF5582DC5 CRC64;
MTHHLIVGGG LAAATAAETL RTEGYDGDIT IVTEEGHPPY QRPPLSKGYL AGREGLDAVI
LHPRHWYADH GMTLRTETTV VTIDPDAHRV ELGDGERVAY DALLLATGSS PRHLPIPGAD
LPGVHTLRRL DDADALASAL RAGGRRLVLV GSGWIGLEVA ATARELGNEV TVLERDPVPL
APALGVRLGA EFARLHTEHG VDLRTSVGVE GIAGTDRATG VVVDGETVPA DLVLIGVGAV
PNTGLAERAG LQVDRGILTD ASLRTSAPDV FAAGDVANAW HPVLGGRLRS EHWANARTAG
PVAARAMLGQ DAVHDGIPYF YTDQYDLGME LSGYAPLMSD AELVIRGDLA AREYIAFWVR
ENRVVGGMNV NVWDVNEKIQ DLVRAQSPVD AAALADPSVA LEELAG
//
