ID A0A367Y8M9_9MICO Unreviewed; 408 AA.
AC A0A367Y8M9;
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:RCK61402.1};
GN ORFNames=DTO57_01780 {ECO:0000313|EMBL:RCK61402.1};
OS Microbacterium sorbitolivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1867410 {ECO:0000313|EMBL:RCK61402.1, ECO:0000313|Proteomes:UP000253508};
RN [1] {ECO:0000313|EMBL:RCK61402.1, ECO:0000313|Proteomes:UP000253508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1.15228 {ECO:0000313|EMBL:RCK61402.1,
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:RCK61402.1}.
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DR EMBL; QORO01000001; RCK61402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Y8M9; -.
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 6..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 323..407
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 408 AA; 43437 MW; 983EC6C628A31ED3 CRC64;
MSTPENVVII GGGLAGAKTA EALREREYAG AVTLVAAEEQ LPYERPPLSK DYLAGKAPFD
DAAVHTAEWY TDNRVDLRLG VRATGIDAAD HRVTLDDGTA LPYDKLVLAT GSAVRRLPLD
GADAENVHYL RTVEDSDAIR ASFGDGKRLV IIGGGWIGLE VASSARAAGT TVTVLEGSSL
TLLRVLGDEV ARVFAGLHRS NGVDLRTEAK VSGIVTDGGR ATGVRLEGGE TIPADAIVIG
IGVSPVTEIA EAAGLAVDNG VLVDASLRTS DPDVYAVGDI ANHDHPVLGH RIRVERWATA
LNQPAVAAAA LLGDDVEYTE LPYFFTDQYD LGCEYIGHAN GAESEVVIRG DLESREFVAF
WLDEHAHIQA AMNVNVWDVI DEIKPLIAER RVVDPKRLAD PAVPFARL
//