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Database: UniProt
Entry: A0A0X3VVN3_9ACTN
LinkDB: A0A0X3VVN3_9ACTN
Original site: A0A0X3VVN3_9ACTN 
ID   A0A0X3VVN3_9ACTN        Unreviewed;       380 AA.
AC   A0A0X3VVN3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KUL48362.1};
GN   ORFNames=ADL22_09650 {ECO:0000313|EMBL:KUL48362.1};
OS   Streptomyces sp. NRRL F-4489.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL48362.1, ECO:0000313|Proteomes:UP000053256};
RN   [1] {ECO:0000313|EMBL:KUL48362.1, ECO:0000313|Proteomes:UP000053256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL48362.1,
RC   ECO:0000313|Proteomes:UP000053256};
RA   Gilbert D.G.;
RL   Submitted (OCT-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:KUL48362.1}.
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DR   EMBL; LLZI01000090; KUL48362.1; -; Genomic_DNA.
DR   RefSeq; WP_066975776.1; NZ_LLZI01000090.1.
DR   AlphaFoldDB; A0A0X3VVN3; -.
DR   STRING; 1609095.ADL22_09650; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000053256; 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   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053256}.
FT   DOMAIN          7..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          236..379
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41740 MW;  349C7BB55AF4DE5B CRC64;
     MKRQIFTEDH DAFRETVRTF LAKEVTPYYA QWEKDGIVSR DAWRAAGRQG LLGLAVPEEY
     GGGGTGDFRY SAVLAEEFTR AGAPGLAIGL HNDIVGPYLT SLATEEQKRR WLPGFCSGET
     ITAIAMTEPG AGSDLQGIRT AAEDRGDHWV LNGSKTFISN GILADLVIVV ARTTPEGGAH
     GLSLLVVERG MPGFERGRNL DKIGQKSQDT AELFFRDVRV PKENLLGELN GAFVHLMTNL
     AQERMAIAIA GIAGAEHVLE LTTRYVKERE AFGRPLAKLQ HIRFEIAEMA TECAVTRTFL
     DRCIADHSAG TLDAVHASMA KWWATELHKR VADRCLQLHG GYGYMTEYPV ARAFTDGRIQ
     TIYGGTTEIM KEIIGRSLLG
//
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