ID A0A1J4NM02_9ACTN Unreviewed; 643 AA.
AC A0A1J4NM02;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OIJ63304.1};
GN ORFNames=WN71_034660 {ECO:0000313|EMBL:OIJ63304.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ63304.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ63304.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
RL Submitted (OCT-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:OIJ63304.1}.
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DR EMBL; LAVA02000107; OIJ63304.1; -; Genomic_DNA.
DR RefSeq; WP_046582386.1; NZ_LAVA02000107.1.
DR AlphaFoldDB; A0A1J4NM02; -.
DR STRING; 1428628.WN71_034660; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000034196; 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; 2.
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 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:UP000034196}.
FT DOMAIN 61..166
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 171..267
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 279..437
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 70257 MW; 37A048E744793E5B CRC64;
MSAPSTKPTV SEREARQVAE AAREQDWRKP SFAKELFLGR FRLDLIHPHP LPSDEAVQRG
EEFLAKLRDF CETKVDPGQI ERDARIPDDV VDGLKEIGAF GMKIETKYGG LGLTQVYYNK
ALALVGSLSP AIGVLLSAHQ SIGVPQPLKL FGTQEQKDAF LPRCARTDIS AFLLTEPDVG
SDPARLATSA VPDGDDYVLD GVKLWTTNGV VADLLVVMAR VPRSEGHKGG ITAFVVETNS
PGITVENRNA FMGLRGIENG VTRFHQVRVP AANRIGPEGA GLKIALTTLN TGRLSLPASC
VAAGKWCLKV AREWSAAREQ WGKPVAQHEA VGSKISFIAA TTFALEAVTD LASQMADEDR
NDIRIEGALA KLYASEMAWL MADELVQIRG GRGFETADSL RARGERAVPA EQMLRDLRIN
RIFEGSTEIM HLLIAREAVD AHLTVAGDLI DPDKSLSDKA KAGAGAGVFY AKWLPRLVAG
QGQVPLSYGE FRRDVDLSGH LRYVERHARK LARSTFYGMS RWQGRMETKQ GFLGRVVDIG
AELFAMSAAC VRAELLRSNG DHGREAYQLA DAFCRQSRLR VEELFGRLWS NTDDLDRTVV
KGVMSGTYEW LEAGIVTLPD DAPWIAETAP GASTAENLHR TIG
//
