ID S6BHK1_PSERE Unreviewed; 388 AA.
AC S6BHK1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAN48574.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:BAN48574.1};
GN ORFNames=PCA10_28420 {ECO:0000313|EMBL:BAN48574.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN48574.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN48574.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN48574.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; AP013068; BAN48574.1; -; Genomic_DNA.
DR RefSeq; WP_016492766.1; NC_021499.1.
DR AlphaFoldDB; S6BHK1; -.
DR STRING; 1245471.PCA10_28420; -.
DR KEGG; pre:PCA10_28420; -.
DR PATRIC; fig|1245471.3.peg.2878; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_5_2_6; -.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000015503; 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; cd00567; ACAD; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
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:SF20; ACYL-COA DEHYDROGENASE FADE28; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000313|EMBL:BAN48574.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 231..369
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 388 AA; 42965 MW; B9B495669D17A11E CRC64;
MNFDFTDEQR LLSDSAERYI RERYSFEERR HLFKNPEGFS RQHWNAFAEM GWLALDIPEE
FGGLGGSSHD LVLLMEQLGS GLVAEPLVDS AVLCARVLRA CDNLELRERL LAQVAAGDVV
LALAHQEQQM RHEYDFELTT KARPVSNGWN LSGGKHRVFH GASADYWVVS AEIEGTGDFA
LFLLERHPVG AAVDSYELID GTRAADITLD HVVIPESALL IRGEAAQEAL EEALDHAVLA
TSAACLGSME QVMAMTADYL KTRVQYGQPL AQFQALQHRM AEMFIETDQA RSMLFSAVRA
VESGDSLQRR LAISGAKVIV TRAQYFVSGQ GIQLHGGIGT TDEYAVGHHY KAAVVYDKRF
GDSEFHLDRS NADLRPADGR PLRSALNA
//