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Database: UniProt
Entry: R9AV53_9GAMM
LinkDB: R9AV53_9GAMM
Original site: R9AV53_9GAMM 
ID   R9AV53_9GAMM            Unreviewed;       675 AA.
AC   R9AV53;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=2,4-dienoyl-CoA reductase (NADPH2) {ECO:0000313|EMBL:EOR05910.1};
GN   ORFNames=I593_02728 {ECO:0000313|EMBL:EOR05910.1};
OS   Acinetobacter tandoii DSM 14970 = CIP 107469.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR05910.1, ECO:0000313|Proteomes:UP000016201};
RN   [1] {ECO:0000313|EMBL:EOR05910.1, ECO:0000313|Proteomes:UP000016201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR05910.1,
RC   ECO:0000313|Proteomes:UP000016201};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOR05910.1}.
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DR   EMBL; AQFM01000040; EOR05910.1; -; Genomic_DNA.
DR   RefSeq; WP_016167759.1; NZ_KE007367.1.
DR   AlphaFoldDB; R9AV53; -.
DR   PATRIC; fig|1120927.3.peg.2656; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   OrthoDB; 8523426at2; -.
DR   Proteomes; UP000016201; Unassembled WGS sequence.
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   PRINTS; PR00469; PNDRDTASEII.
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;
FT   DOMAIN          7..332
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          377..640
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   675 AA;  73722 MW;  00D985E61187B078 CRC64;
     MSNYPHLLAP LDLGFTTLKN RVLMGSMHVG LEEAPGGYDR MAAFYAERAK GGVGLIVTGG
     ISPNDHGLTF KGGSKLDTRE EAEHHKVITQ AVHDAGGKIA LQILHTGRYS YQKDIVAPSA
     IQAPINPSRP KELSSAEVQQ TIDDFVNCAK LSQYAGYDGV EIMGSEGYLI NEFIAARTNH
     RDDEWGGSYE KRIRFPIEIV KRTREAVGEN FIIIYRLSML DLVEGGSSLE EVIHLAKEIE
     KAGATIINTG IGWHEARIPT IATKVPRAAF TWVTKKLKGS VNIPLVTSNR INTPEMAEHV
     LASGDADIVS MARPMLADPE FVLKAEQGRS DEINTCIGCN QACLDHIFSM KIATCLVNPR
     ACYETELIFK EAGQAKNIAV IGAGPAGLSF ATYAAERGHN VTIFEAANQI GGQFNIAKTV
     PGKEEFYETL RYFKRKIELL QPKIKLQLNH KATYEELSQA NFDDIVVATG VTPRELSFEG
     IDHPKVLSYL EVLRERKPVG KRVAVIGAGG IGFDTAEYLS HEGESGSLNP QKFYDEWGID
     THYNDVGGLK QPQVEASERE IFLLQRKPTS VGAGLGKTTG WIHRAGLKNR DVQMIAGASY
     EKVDDQGLHI IVNDKSMILD VDNVVICAGQ EPFTAMFDQL KADGKAVHLI GGAKEAGELD
     AKRAIRQGAE LAAVI
//
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