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Database: UniProt
Entry: A0A3B0AW73_9MICO
LinkDB: A0A3B0AW73_9MICO
Original site: A0A3B0AW73_9MICO 
ID   A0A3B0AW73_9MICO        Unreviewed;       389 AA.
AC   A0A3B0AW73;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:RKN64670.1};
GN   ORFNames=D7252_18750 {ECO:0000313|EMBL:RKN64670.1};
OS   Microbacterium sp. CGR2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1805820 {ECO:0000313|EMBL:RKN64670.1, ECO:0000313|Proteomes:UP000278458};
RN   [1] {ECO:0000313|EMBL:RKN64670.1, ECO:0000313|Proteomes:UP000278458}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGR2 {ECO:0000313|EMBL:RKN64670.1,
RC   ECO:0000313|Proteomes:UP000278458};
RA   Mandakovic D., Cintolesi A., Maldonado J., Cortes M.P., Mendoza S.,
RA   Aite M., Gaete A., Saitua F., Cambiazo V., Agosin E., Siegel A., Maass A.,
RA   Gonzalez M., Latorre M.;
RT   "Comparative genome-scale metabolic modeling of two Microbacterium species
RT   isolated from Atacama Desert.";
RL   Submitted (SEP-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:RKN64670.1}.
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DR   EMBL; RBHX01000002; RKN64670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0AW73; -.
DR   OrthoDB; 1145at2; -.
DR   Proteomes; UP000278458; 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; PR00469; PNDRDTASEII.
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:UP000278458}.
FT   DOMAIN          9..295
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          315..382
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   389 AA;  40438 MW;  ED5675BCB9385830 CRC64;
     MGSELAMTRT LIVGAGAAGL TCAKHLRQLD ETRTITVLDK DPDVPYERPP LSKALSGAGS
     VSAGTDELKG AGIDVVFGTA VGVTVADQLL HTSGGDLGYD ELVLAPGSRP HRPSWVSEEV
     HALHSLDDSR RLRQAVSAAG SAVVIGGGFV GAELAASLVS AGVTTTFVFR EDALFRNRLG
     QAASDLLTRL HTEAGVRLIP NGTVADVQSG HPAQVHLTDG TTLHADLVVA GIGSHPDTAW
     LGDSGVLADD DTIRTDACLH TSAPGVAAAG DSVSWTGFDG SVMRSAHWTT ARSHGRHIAI
     DLAAGTRTPF LEPPYFWSMQ HGSLLQGIGH VDPQISEIEV LEGTGPKPGL LARYLIDGEL
     VGAVAINHPQ GFMAARADVE KHAASTLIR
//
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