ID C3KC90_PSEFS Unreviewed; 389 AA.
AC C3KC90;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Oxidoreductase (EC) {ECO:0000313|EMBL:CAI2797505.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CAI2797505.1, ECO:0000313|EMBL:CAY49516.1};
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CAY49516.1};
GN OrderedLocusNames=PFLU_3290 {ECO:0000313|EMBL:CAY49516.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY49516.1};
RN [1] {ECO:0000313|EMBL:CAY49516.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY49516.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2797505.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2797505.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OV986001; CAI2797505.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY49516.1; -; Genomic_DNA.
DR RefSeq; WP_012724452.1; NC_012660.1.
DR AlphaFoldDB; C3KC90; -.
DR PATRIC; fig|216595.4.peg.3451; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_0_6; -.
DR OrthoDB; 7316074at2; -.
DR Proteomes; UP001152918; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd01159; NcnH; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CAY49516.1}.
FT DOMAIN 236..367
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 389 AA; 43031 MW; 23D5AC80CA645AD7 CRC64;
MKKPNPLLED LTSILPTIAA NAFMAEQDRK VPAENIALLK SIGLHRAFQP KAFGGMELSL
PQFADCIALL AGACASTAWA MSLLCTHSHQ LALFSAQLQQ EVWGTDPNAT ASSSIAPFGR
TEEVDGGVLF SGEMGWSSGC DHAEWAIVGF RRNNAQGTQD YCFAVLPRSD YQIRDDWFAA
GMKGSGTKTL IIDKARVPEH RIQKAKDMME GKSAGFGLYP DSKIFYSPYR PYFASGFSTV
SLGVAERMLE VFREKTKTRV RAYTGAAVGA ATPALMRLAE STHQVAAARA FLEKTWNEHA
EHSEQQRYPS RETLAFWRTN QAYATKMCIQ AVDRLFEAAG GNAWFEHNEM QRLFRDSHMT
GAHAYTDYDV CAQILGRELM GLEPDPSMI
//
