ID U5WPP0_MYCKA Unreviewed; 354 AA.
AC U5WPP0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AGZ49886.1};
GN ORFNames=MKAN_06060 {ECO:0000313|EMBL:AGZ49886.1};
OS Mycobacterium kansasii ATCC 12478.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ49886.1, ECO:0000313|Proteomes:UP000017786};
RN [1] {ECO:0000313|EMBL:AGZ49886.1, ECO:0000313|Proteomes:UP000017786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ49886.1,
RC ECO:0000313|Proteomes:UP000017786};
RG McGill University Mycobacterium genome consortium;
RA Veyrier F.J., Behr M.A.;
RT "Genome sequence of Mycobacterium kansasii.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; CP006835; AGZ49886.1; -; Genomic_DNA.
DR RefSeq; WP_023366132.1; NC_022663.1.
DR AlphaFoldDB; U5WPP0; -.
DR GeneID; 29699809; -.
DR KEGG; mkn:MKAN_06060; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_5_1_11; -.
DR OrthoDB; 3459196at2; -.
DR Proteomes; UP000017786; 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; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
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}.
FT DOMAIN 14..107
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 200..339
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 354 AA; 37742 MW; 097E7D925B1CF32C CRC64;
MDRFELRRLD YSLSEDHIAL QSAYKQFFKT HCSIETVRAA EPSGFDKSLW ERLCGMGATT
MALPESAGGD GATLVDLTLV AEEIGRSLAP VPWIDHVCAT RLLARLGMLD AETAALANGE
QLAALDPRID GGPGRRLIPA GSIAGRVVVV DRDRILSLTF GTQPAKVDNI GRLPMAWVDP
AAADSRTVVA RGSEALANYQ RALDEWRLLM AAALVGLVEE TMTIAAEFAK TRYTLGVPIA
TLQGISHPLA NMAITVHSGR NLVRRAAWFL DNEPGERPEL APAAFLFMAE EAAKAATMAV
HIQGGLGVSA EAAATAYLVR ARGWPLAGGD PGACARRIAE IVATRETASR AACF
//
