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
//