ID A0A384I5Y2_9ACTN Unreviewed; 388 AA.
AC A0A384I5Y2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PZT75826.1};
GN ORFNames=DNK56_20655 {ECO:0000313|EMBL:PZT75826.1};
OS Streptomyces sp. AC1-42W.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2218666 {ECO:0000313|EMBL:PZT75826.1, ECO:0000313|Proteomes:UP000249154};
RN [1] {ECO:0000313|EMBL:PZT75826.1, ECO:0000313|Proteomes:UP000249154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC1-42W {ECO:0000313|EMBL:PZT75826.1,
RC ECO:0000313|Proteomes:UP000249154};
RA De Leon M.P., Montecillo A.D., Siringan M.A.T., Kim S.-G., Rosana A.R.R.;
RT "Near complete genome sequences of Streptomyces sp. strains AC1-42W
RT isolated from bat guano of Cabalyorisa Cave, Pangasinan, Philippines.";
RL Submitted (JUN-2018) 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:PZT75826.1}.
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DR EMBL; QKWY01000002; PZT75826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384I5Y2; -.
DR Proteomes; UP000249154; 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 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; 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; PTHR48083:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06510)-RELATED; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000249154}.
FT DOMAIN 9..119
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 233..375
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 388 AA; 41336 MW; 16AB1127254177DA CRC64;
MSTSTILETE EHQALRAAVA ALGKRYGREY MTGLVSGGGH PRELWADAAK AGFLGVNLPE
EYGGGGAGMA ELSIVLEELG ASGSPLLMMI VSPAICGTVI ARFGTDEQKR QWLPGLADGS
LTMAFGITEP DAGSNSHRIT TTARRDGDHW LLTGRKVFVS GVDIADATLI VGRTEDARTG
KLKACLFIVP RDTPGFQRSP IDMEVQAPEK QFELVLDDVR LPADALVGDE DAGLLQLFAG
LNPERIMTAA FGIGMGRYAL GRAVEYAKTR QVWKEPIGAH QAIAHPLAQA HIELELARLM
MQKAARLYDA GDDLGAGEAA NMAKYAAGEA CVRAVDQAVH TLGGNGLTRE YGLASLITGA
RVARIAPVSR EMILNYVSHQ TLGLPKSY
//
