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Database: UniProt
Entry: A0A1B1B033_9ACTN
LinkDB: A0A1B1B033_9ACTN
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ID   A0A1B1B033_9ACTN        Unreviewed;       598 AA.
AC   A0A1B1B033;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ANP52203.1};
GN   ORFNames=AVL59_23985 {ECO:0000313|EMBL:ANP52203.1};
OS   Streptomyces griseochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP52203.1, ECO:0000313|Proteomes:UP000092659};
RN   [1] {ECO:0000313|EMBL:ANP52203.1, ECO:0000313|Proteomes:UP000092659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP52203.1,
RC   ECO:0000313|Proteomes:UP000092659};
RA   Wu L.;
RT   "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT   Blasticidin S producer.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP016279; ANP52203.1; -; Genomic_DNA.
DR   RefSeq; WP_067307917.1; NZ_JAGGLP010000047.1.
DR   AlphaFoldDB; A0A1B1B033; -.
DR   STRING; 68214.AVL59_23985; -.
DR   KEGG; sgs:AVL59_23985; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000092659; Chromosome.
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; 1.
DR   InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF3; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_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}.
FT   DOMAIN          6..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          42..156
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          162..265
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          292..457
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          482..594
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   598 AA;  64962 MW;  51B73503DE373D48 CRC64;
     MASLLLSRRD LDFLLHEWLD VESLTARPRF ADHSRETFDA VLDLSETIAA RHFAPHNKKN
     DAQEPRFDGE RVHIIPEVEE ALKVFAGAGL IGGGMDHEVG GMQLPSVVAN ACFAWFQAAN
     VGTAAYPFLT IGNANLLLAH GTPGQIDTYV RPMVEGRFSG TMCLSEPQAG SSLADVRTRA
     EQADDGTYRL FGNKMWISGG DHELTENIVH LVLARIPGGP PGVKGLSLFI VPKVLVEADG
     TLGERNDVAL AGLNHKMGYR GTTNTLLNFG EGAFRPGGTP GAVGFLVGEP HHGLSYMFHM
     MNEARIGVGL GATALGYTGY LHALDYARTR PQGRPLMARD ATIPQIPIVG HPDVRRMLLA
     QKSYVEGALA LILYCGRLLD DERTAPTADE RASAGLLLDM LTPIAKSWPS QWCLEANNLA
     IQVHGGYGYT REYNVEQFYR DNRLNPIHEG THGVHGLDLL GRKVVMDGGA GLRLLIETVS
     MTTARAVAAE GQVAGFGRQL DASVARVAAV TRRLWEAGDA ETALANASVY LESVGHVVVA
     WMWLEQMLAA GGRGGAFYEG KRRAGQYFFR YELPRTEAQF ALLESLDRTT LDMPADCF
//
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