ID A0A3N4R7A8_9ACTN Unreviewed; 382 AA.
AC A0A3N4R7A8; A0A8G1UFT1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:RPE29082.1};
GN ORFNames=EDD38_6230 {ECO:0000313|EMBL:RPE29082.1}, EDD39_5622
GN {ECO:0000313|EMBL:ROR37476.1};
OS Kitasatospora cineracea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=88074 {ECO:0000313|EMBL:RPE29082.1, ECO:0000313|Proteomes:UP000266906};
RN [1] {ECO:0000313|Proteomes:UP000266906, ECO:0000313|Proteomes:UP000267408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44780 {ECO:0000313|EMBL:ROR37476.1,
RC ECO:0000313|Proteomes:UP000267408}, and DSM 44781
RC {ECO:0000313|EMBL:RPE29082.1, ECO:0000313|Proteomes:UP000266906};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-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:RPE29082.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RJVJ01000002; ROR37476.1; -; Genomic_DNA.
DR EMBL; RKQG01000002; RPE29082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4R7A8; -.
DR Proteomes; UP000266906; Unassembled WGS sequence.
DR Proteomes; UP000267408; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..216
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 228..376
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 382 AA; 40592 MW; 7E9E4CF57A73300B CRC64;
MDLELTEEQA AVRELAAAFT DREIVPFAAE WDRAESIDLG IIGKLGDLGF LGLTLPEEYG
GSGGDHLAYC LVLEELGRGD SSVRGVVSVT LGLVAKSVNA FGTEEQKRQW LPRLCSGEAL
GCFALTEPGT GSDAANLTTR AERDGEDWLI SGAKMFITNG TWADVALVFA RTGGPGHRGV
TAFLVPTDAP GFERRLVHGK LGLRGQATAE LSFDRVRVPD GARLGEVGKG FTVAMAALAK
GRMSVAAGCV GIAQAALDAA VRYAGEREQF GKPIAAHQLV QELLADIAVD VDAARLLTWR
VADLIDRGQP FATESSVAKL YASEAAVRCA NNALQVFGGY GFIDEYPVGK YLRDARVMTL
YEGTSQIHKL LIGRSLTGVN AF
//
