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Database: UniProt
Entry: D9T026_MICAI
LinkDB: D9T026_MICAI
Original site: D9T026_MICAI 
ID   D9T026_MICAI            Unreviewed;       675 AA.
AC   D9T026;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=NADH:flavin oxidoreductase/NADH oxidase {ECO:0000313|EMBL:ADL47262.1};
GN   OrderedLocusNames=Micau_3736 {ECO:0000313|EMBL:ADL47262.1};
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS   129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL47262.1, ECO:0000313|Proteomes:UP000001908};
RN   [1] {ECO:0000313|EMBL:ADL47262.1, ECO:0000313|Proteomes:UP000001908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC   {ECO:0000313|Proteomes:UP000001908};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Hirsch A.M., Woyke T.;
RT   "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP002162; ADL47262.1; -; Genomic_DNA.
DR   RefSeq; WP_013286886.1; NC_014391.1.
DR   AlphaFoldDB; D9T026; -.
DR   STRING; 644283.Micau_3736; -.
DR   KEGG; mau:Micau_3736; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_2_11; -.
DR   OrthoDB; 3169239at2; -.
DR   Proteomes; UP000001908; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT   DOMAIN          9..342
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
SQ   SEQUENCE   675 AA;  71170 MW;  50D174BF482BC685 CRC64;
     MPDDKLLALL SPTRLGRLTL RNRVFVPGHT TNFGLNNVPT RRHVAYHAER ARGGAGLIIT
     EAIRVHPTSA GRSISLGSFD DSSIPAYAAV TEAVHEHGAR MFAQIMHAGR QANGDATRTA
     AWSSSPVPWA AGSHVPHAMG RRDIAVVVEA FAAAARRMRE AGFDGLEVHA GHGHLLQQFL
     SPHTNTRDDA YGGSLDNRMR LTREVLTAVL AAAPELPVGL RVSADEFLPG GLDPAAVLEI
     VGKLRAEFPL AYVHVSHSAY HGSWSLATQM ADMSFGHAPF RHHAALFKQE FPDLPVLAVC
     RLDSLPEAAE LVAAGEADLV GLARPHIADP HLVRKAEQGR QHEVRACLAC NQGCIGRLET
     SLPISCVVNP EVGAEREWAD AWPELPGPSG ARDVLVVGGG PAGLEAALSA HRAGHRVTVV
     EARDRLGGQV EVAARVPGRE RLGLLTRDLA RDVAAAGIPV RLGHRAGVED VLSGGYQDVV
     LATGSRPARR DLPGGPPVVD IWQAVDHLAD PGYRPDGAVV VLDDEGTWSA ASVAEAFARR
     GARVHLVSPT ATVSAKITTY SRLALLKRFA DLGIAVHPMR TARAAGAGAV ALGGPLAGGE
     TIVEGVTTVV DGGSAQAADE LYRQLDALPD GPRVHVVGDA NAPRSAFEAV YEGRMAGAFL
     GAFDTAAAER VRYAH
//
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