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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//