(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJS3_PSEPF

ID   Q3KJS3_PSEPF            Unreviewed;       397 AA.
AC   Q3KJS3;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 96.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:ABA71983.1};
GN   OrderedLocusNames=Pfl01_0239 {ECO:0000313|EMBL:ABA71983.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71983.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71983.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71983.1,
RC   ECO:0000313|Proteomes:UP000002704};
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).
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DR   EMBL; CP000094; ABA71983.1; -; Genomic_DNA.
DR   RefSeq; WP_011331943.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0239; -.
DR   EnsemblBacteria; ABA71983; ABA71983; Pfl01_0239.
DR   KEGG; pfo:Pfl01_0239; -.
DR   eggNOG; ENOG4106G3Z; Bacteria.
DR   eggNOG; ENOG410XQ4C; LUCA.
DR   HOGENOM; HOG000219184; -.
DR   OMA; KYHAVGN; -.
DR   BioCyc; PFLU205922:G1G4S-240-MONOMER; -.
DR   Proteomes; UP000002704; 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   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR013107; Acyl-CoA_DH_C_dom.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR023922; S04_starv_induced_SfnB.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   TIGRFAMs; TIGR04022; sulfur_SfnB; 1.
PE   4: Predicted;
DR   PRODOM; Q3KJS3.
DR   SWISS-2DPAGE; Q3KJS3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704}.
FT   DOMAIN       36    119       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      131    213       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      240    372       Acyl-CoA_dh_2. {ECO:0000259|Pfam:
FT                                PF08028}.
SQ   SEQUENCE   397 AA;  43390 MW;  EEBF53BF34344BF8 CRC64;
     MTFSHPVAVI TSDEQALIVA SDLAEDFQRD SNLRDRERRL PLPELDVFSR SGLWGISVPK
     EYGGAGVSNV TLAKVIALIA RADGSLGQIP QNHFYALEVL RVNGSHEQKQ RLYAEVLAGQ
     RFGNALAELG TRTAHDRVTR LERDGSGYRI NGRKFYATGA IYAQRIPTSV VDENGVQQLA
     FVPRDSKGLT VIDDWSGFGQ RTTGSGSVVF ENVYVAAEDV IPFQSAFERP TPVGPLAQIL
     HAAIDTGIAR AAYEDALHFV RSKTRPWIDS GNDKATEDPL TLKSFGHLSI RLHATEALLE
     RAGEFLDAAQ AETNAETVAA ASIAVAEARA ISTEISLAAG STLFELAGSQ ATLIEHGLDR
     HWRNARVHTL HDPVRWKYHA VGNYYLNDEN PPLRGTI
//

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