ID A0A117IVA9_9ACTN Unreviewed; 383 AA.
AC A0A117IVA9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KUH37040.1};
GN ORFNames=ATE80_20465 {ECO:0000313|EMBL:KUH37040.1};
OS Streptomyces kanasensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH37040.1, ECO:0000313|Proteomes:UP000054011};
RN [1] {ECO:0000313|EMBL:KUH37040.1, ECO:0000313|Proteomes:UP000054011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX01 {ECO:0000313|EMBL:KUH37040.1,
RC ECO:0000313|Proteomes:UP000054011};
RA Zhang G., Han L., Feng J., Zhang X.;
RT "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT kanasensis ZX01.";
RL Submitted (NOV-2015) 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:KUH37040.1}.
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DR EMBL; LNSV01000057; KUH37040.1; -; Genomic_DNA.
DR RefSeq; WP_058943695.1; NZ_LNSV01000057.1.
DR AlphaFoldDB; A0A117IVA9; -.
DR STRING; 936756.ATE80_20465; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000054011; 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 PIRSF; PIRSF016578; HsaA; 2.
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:UP000054011}.
FT DOMAIN 11..114
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 119..214
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 228..370
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 383 AA; 40752 MW; D1189A61EA6A8D9F CRC64;
MTAVTGTPFE TAEQQALRTA VAALGRRHAD THEEHPEVLW AEAGRLGYLG VNLPEEYGGG
GGGVAELAIV LEELGTAGCP LLLMIVSPAI CGTVIARFGT DEQRRRWLPG LADGSRIMAF
GITEPDAGSN SHRITTTARR TPGGWVLSGR KVFVSGVDLA EETMIVGRTA DARTGALKPC
LFVVPRDAPG FRRTAIDMEL RAREKQFELT LDDVRLPADA LVGDEDAGLL QLFAGLNPER
VMTAAFALGM GRFALARAVA YAKERQVWKA PIGAHQAIAH PLAASHIELE LARLMTRRAA
ALCDAGDDVG AGEAANMAKY AAAEACVRAV DRAVHTLGGN GLTREYGLGR LVTASRVARI
APVSREMILN YVSHQSLGLP KSY
//
