ID A0A177Y783_9NOCA Unreviewed; 379 AA.
AC A0A177Y783;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OAK51373.1};
GN ORFNames=A3K89_12300 {ECO:0000313|EMBL:OAK51373.1};
OS Rhodococcus kyotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK51373.1, ECO:0000313|Proteomes:UP000077519};
RN [1] {ECO:0000313|EMBL:OAK51373.1, ECO:0000313|Proteomes:UP000077519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB10 {ECO:0000313|EMBL:OAK51373.1,
RC ECO:0000313|Proteomes:UP000077519};
RA Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT "Genome sequence of Rhodococcus kyotonensis KB10.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:OAK51373.1}.
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DR EMBL; LVHI01000039; OAK51373.1; -; Genomic_DNA.
DR RefSeq; WP_068431296.1; NZ_LVHI01000039.1.
DR AlphaFoldDB; A0A177Y783; -.
DR Proteomes; UP000077519; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000077519}.
FT DOMAIN 10..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 124..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 231..372
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 379 AA; 42011 MW; D34EA360018DFD49 CRC64;
MDLDFDSDTV RFREKVREFL RDNIPERPLR SMDTADGFEA HREWERMLAR HRYSVVSWPR
DLGGRDASVL EWLVFEEEYY AAEAPGRVSQ NGIFLLAPTL FAHGTDEQLR RILPRMAAAD
DIWAQAWSEP EAGSDLAGIR SSAHRTDGGW LLRGQKTWSS RAGFADKAFG LFRSDPAAER
HRGLTYCMFS LTADGVTVRP IPQLNGESGF AEIFLDDVFV PDDDVLGAVH DGWRVAMSTS
SNERGMSLRS PGRFVAAADR LVRLFREHGD ASDTAVAHRV VDAWIGAQAY RLHTFGTATT
LADGGSLGAE SSLTKVFWSE LDVALHETAL DVLGTDAEVR GPWTDGFVFS LSGPIYAGTN
EIQRGVIAER LLGLPKAHR
//
