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Database: UniProt
Entry: F4CUN3_PSEUX
LinkDB: F4CUN3_PSEUX
Original site: F4CUN3_PSEUX 
ID   F4CUN3_PSEUX            Unreviewed;       957 AA.
AC   F4CUN3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=NADPH dehydrogenase {ECO:0000313|EMBL:AEA26347.1};
DE            EC=1.6.99.1 {ECO:0000313|EMBL:AEA26347.1};
GN   OrderedLocusNames=Psed_4184 {ECO:0000313|EMBL:AEA26347.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS   CB1190).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA26347.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA26347.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA   Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA   Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT   strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP002593; AEA26347.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CUN3; -.
DR   STRING; 675635.Psed_4184; -.
DR   KEGG; pdx:Psed_4184; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   eggNOG; COG4126; Bacteria.
DR   HOGENOM; CLU_308325_0_0_11; -.
DR   OrthoDB; 3169239at2; -.
DR   Proteomes; UP000007809; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036361; F:racemase activity, acting on amino acids and derivatives; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.12500; -; 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; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR003953; FAD-binding_2.
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; PF01177; Asp_Glu_race; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEA26347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT   DOMAIN          13..341
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          400..439
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   957 AA;  102992 MW;  A0FCCF38BBF83CF3 CRC64;
     MTDRNDAPPP ERVFRPLTLG PVTLRNRIFV SAHTTNLGER HEVSDRLVAY HRERAAGGVG
     LVVTEGLRVH PTSLKRPEAL SVWSDDAVAP LRRLTAAVQG EGAAIFAQIL HSGREAADDY
     TRTPSWGPSP IPWSRGAAVP HAMTTDEIDE LVDCFAGGVL RAAAAGFDGV EIHLGHGHLL
     QQFLSPISNG RDDEYGGTPA NRARLVERVL TRTRGLVPAH MAFGVRISAE EFVDGGLGVD
     VMSQYAAQWA SRYRLDFVDV SHSAYVGGPS LSTQMADMSH GPAPFAHLGK AVRDRLPDDV
     ATLLACRIDS LDVAEDVLAA GCADATAMTR AHIADPGLNR KHRGGEVVRR CTSCNQLCIG
     RSSGGLPISC VVNPEVGLEE AWREAYAAAD RVVTGGRPRL LVVGGGPAGM EAALTATRWA
     DVTLVEREPA LGGALRTARA LHGRSGWARL VEDQERTCRE CGVELRQGVA FDAGLLTAEP
     WDGIVLATGA VVGPRWSDDR DPVRCFGSGV PDPAGVRRAA VHDDRGGWEA WGVVAHLVHH
     GVETHYVTPL QSLAPGVTIY SRLGLLAGLR ASDLLHVHLM TTVSGWRDRV LTLRASLPDT
     ETAVADVDAL WDAGVATPAA PRRLPVPHRV VGDAYAPRGA GWAVYSGRLG ALRILADIRH
     RDDPVARSTA QRGLDADRRV AHVVPGRTVK IWFQKHTIIG RNPWLDETYP RHATAMLGDR
     ADVTFVGLPG AVYDDQIPAD YVRFGQIEVF FSWYFASQAV KAERAGYDAY VIGTSQDPGL
     AMARSLVSIP VLAYGETAFT LARTHGLRFG VVGFIPELEE ALTANIRALG LADSCVGFRY
     LEGGRDLVTS ATRDGRTDAL AAAMDEAATT LRRTGAQCIV PGEGLPNEML WAAGIHEVGG
     LPVIDCDGLV MLTAEMHARA RRLRVWAPDD DSYDTRRAPD EVIDRMTEIF SPGGGRW
//
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