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Database: UniProt
Entry: A5W492_PSEP1
LinkDB: A5W492_PSEP1
Original site: A5W492_PSEP1 
ID   A5W492_PSEP1            Unreviewed;       650 AA.
AC   A5W492;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=NADH:flavin oxidoreductase/NADH oxidase {ECO:0000313|EMBL:ABQ78952.1};
GN   OrderedLocusNames=Pput_2820 {ECO:0000313|EMBL:ABQ78952.1};
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ78952.1};
RN   [1] {ECO:0000313|EMBL:ABQ78952.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ABQ78952.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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; CP000712; ABQ78952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5W492; -.
DR   KEGG; ppf:Pput_2820; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_2_6; -.
DR   OMA; IMESADG; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd04734; OYE_like_3_FMN; 1.
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; IPR023753; FAD/NAD-binding_dom.
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; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
FT   DOMAIN          8..338
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          388..621
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   650 AA;  70387 MW;  E6580E6119B9C188 CRC64;
     MQTAFPHLFE PLQIRGKRLK NRIMSTGHDT CLPTDNLVND KLIAYQRDRA AGGVGLIVLQ
     VAGVHDSARY TSHVLMATDD ACIDGYRQLA EACHAHGTVV LSQLFHPGRE IMESADGLLA
     VAYSASAVPN ERFRVMPRAL DQAMIDEIVQ GYAGAARRLH QAGLDGVEVV ASHGYLPAQF
     LNPRVNVRSD GYNGDLDQRL RFLREVLAAV RAATDEQFII GLRISADERD SQGLSEDESL
     AAAVALQGQL DYLHIVAGTS ASLGGAVHIV PPMAIEPAYL AREAGTFKQQ LAIPLFVTGR
     INQPQEAELI LARGQADVCG MTRALICDPS MPGKTERGQV EDVRACIACN QACIGHFHRG
     LPISCIQRPE TGRELQYGHL TPTSSPKRIM VAGGGPAGMK AAAVAAARGH QVTLYEAGPQ
     LGGQVLLAQL LPRRSEFGGA STNLQREMAL AGVEVVRNTR VDRALVERER PDLVIAATGA
     TPYWPAFERT GELQVVDAWQ VLRNEVKPGR SVLVIDWRCD WIGPGIAERL VREGHQVQLA
     VNGTHCGESL PLYVRDQLAG ELHRLGIPVT PYARLYGSDD NTVYLQHTAS GDPMIFEGID
     TLVLCMGHQP QDRLATELAG VVDVRRIGDC LAPRTAEEAI HDGLTVAWAL
//
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