ID A0A367Y289_9MICO Unreviewed; 403 AA.
AC A0A367Y289;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:RCK60006.1};
GN ORFNames=DTO57_07645 {ECO:0000313|EMBL:RCK60006.1};
OS Microbacterium sorbitolivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1867410 {ECO:0000313|EMBL:RCK60006.1, ECO:0000313|Proteomes:UP000253508};
RN [1] {ECO:0000313|EMBL:RCK60006.1, ECO:0000313|Proteomes:UP000253508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1.15228 {ECO:0000313|EMBL:RCK60006.1,
RC ECO:0000313|Proteomes:UP000253508};
RA An D.;
RT "Microbacterium endoborsara sp. nov., a novel actinobacterium isolated from
RT Borszczowia aralocaspica.";
RL Submitted (JUL-2018) 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:RCK60006.1}.
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DR EMBL; QORO01000002; RCK60006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Y289; -.
DR OrthoDB; 1145at2; -.
DR Proteomes; UP000253508; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000253508}.
FT DOMAIN 1..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 318..403
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 403 AA; 42668 MW; 015290537CFD87C4 CRC64;
MRVIIIGGGL AAATAAEGLR ERGFDGQIDV VTAETHRPYQ RPPLSKGYLL GSEGLDEVYA
HPVGWEAEHD VTLHVADPAV RIADGVVALE SGAELGFDRL ILATGASPRP LDVPGADAAG
VRMLRTIDDA DGLRADLLGG GRRVVLIGSG WIGLELAAAA RELGNDVTIV SPDRVPLAKA
LGDEMGEMFL ELHREHGVTF LPERRVTAVE AGENGSVVAV RTDDESIPAD LVIVGIGAEL
NTALAEEAGL AVDNGVLVDE RMNTSVPGIL AIGDIANALH PVLGERIRTE HWATAIATGK
IAASTITGGD ATLDGVPYFF TDQYDLGMEF SGYAPLMTGA HLVIRGDRAG REFIAFWVAD
GRVVAGMNVN VWDVNEQVQH LIRERVEIDE AQLADPSVPL EEL
//
