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Database: UniProt
Entry: A0A1H5PUG6_9ACTN
LinkDB: A0A1H5PUG6_9ACTN
Original site: A0A1H5PUG6_9ACTN 
ID   A0A1H5PUG6_9ACTN        Unreviewed;       401 AA.
AC   A0A1H5PUG6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:SEF16851.1};
GN   ORFNames=SAMN05216533_8019 {ECO:0000313|EMBL:SEF16851.1};
OS   Streptomyces sp. Ag109_O5-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEF16851.1, ECO:0000313|Proteomes:UP000198812};
RN   [1] {ECO:0000313|EMBL:SEF16851.1, ECO:0000313|Proteomes:UP000198812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEF16851.1,
RC   ECO:0000313|Proteomes:UP000198812};
RA   de Groot N.N.;
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}.
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DR   EMBL; FNTQ01000001; SEF16851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5PUG6; -.
DR   STRING; 1855349.SAMN05216533_8019; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000198812; 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   GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198812}.
FT   DOMAIN          26..138
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          142..235
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          250..394
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   401 AA;  44071 MW;  C3FA99BAB2A5DE8F CRC64;
     MTTTPPALSD DLLAADFYLY EALLPDEERT ILGKARAFLR DEVKPLVNGY WDKGEFPVEL
     IERFRGSGLT ALSYEGYGDH LPATSHLLGG MLAMEMSRVD ASVATFFGVH NGLSFYSILT
     GGDQEQRERW LPAMASMEKI GAFAMTEPLG GSDVSGGMRT TAERRGGTWV LNGAKRWIGN
     ATFADHVVVW ARDVDDNQVK GFVVEKGTPG FVPVKIEGKI ALRIVENAEI TLTDVRVPEA
     DRLQNINSFR DVAEILRFTR SGVAWQALGV MIGAYELALG YAKERRQFGR PIAGFQMVQD
     LLVKSLGDIT ASWGMLVQLA RLQDQGIFRD DHSALAKGFT TSRMREVVAA GREIFGGNGI
     VLDYDVARFF ADAEALYSYE GTRQMQTLIV GKSITGQSAF V
//
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