ID Q8F450_LEPIN Unreviewed; 669 AA.
AC Q8F450;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=2,4-dienoyl-CoA reductase (NADPH) {ECO:0000313|EMBL:AAN49396.1};
GN Name=nemA {ECO:0000313|EMBL:AAN49396.1};
GN OrderedLocusNames=LA_2197 {ECO:0000313|EMBL:AAN49396.1};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN49396.1, ECO:0000313|Proteomes:UP000001408};
RN [1] {ECO:0000313|EMBL:AAN49396.1, ECO:0000313|Proteomes:UP000001408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601 {ECO:0000313|EMBL:AAN49396.1,
RC ECO:0000313|Proteomes:UP000001408};
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; AE010300; AAN49396.1; -; Genomic_DNA.
DR RefSeq; NP_712378.1; NC_004342.2.
DR RefSeq; WP_000877554.1; NC_004342.2.
DR AlphaFoldDB; Q8F450; -.
DR STRING; 189518.LA_2197; -.
DR PaxDb; 189518-LA_2197; -.
DR EnsemblBacteria; AAN49396; AAN49396; LA_2197.
DR KEGG; lil:LA_2197; -.
DR PATRIC; fig|189518.3.peg.2190; -.
DR HOGENOM; CLU_012153_1_1_12; -.
DR InParanoid; Q8F450; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02930; DCR_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.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001408}.
FT DOMAIN 5..329
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 376..628
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 669 AA; 73418 MW; 4B1C73AB1CDDDD23 CRC64;
MKYSEIFQPI QIGSIVLPNR VIMGSMHLGL EGMPMTADRM IAFYGRRFDG GASFITTGGI
AVNHEGRGSN IFFNFQREED CKELSVVANS LKSKGIFCAQ LFHAGRYAYH RELVAPSALR
APINRYVPKA LSEEEAWKTV EDFGDSALKA KEVGFGAVEV MGSEGYLVNQ FFSPVTNHRE
DFFGGSSEKR MNFAIEVMKN IRKKVGKDFP VVYRMSGIDL IPGNPTFEEV ILLAEKLKEA
GADALNIGIG WHESRIPTIS MLVPRGAWAK ISGKIKAKVK DIPIIASNRV NMPETMSRIL
KDQEADILSM ARPFLADPDI LNKIKANQEE RINTCIACNQ ACLDHTFKEQ MVSCLVNPSA
NRELELSKLK KADKKHVVVV GSGPGGLESA RISAIRGHKV TVLEATDKIG GQLNLAAQIP
GKSEFLETIR YFKNELKNLG VEIHFGYQAT LDSILVLKPD AVIFATGVKP REFTLPGIEK
KKTASYADYL SGKFQPGNKV VVIGGGGIGC DVAHKLTEED SSTIDSYFHR YNVTSYTNAQ
IQKEKPNRKV SIFRRSGKIG SGLGATTAWA LLQELESKEV GFYTSLSYKE VTDQGLVIET
KKDGAQTIEC DSIILCAGQL SEVSLYEEFK SKVPEIPSYL IGGAKDASGI DAKRAMLEGF
EAAIEIGVN
//
