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Database: UniProt
Entry: A0A0N0TJQ5_9ACTN
LinkDB: A0A0N0TJQ5_9ACTN
Original site: A0A0N0TJQ5_9ACTN 
ID   A0A0N0TJQ5_9ACTN        Unreviewed;       397 AA.
AC   A0A0N0TJQ5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE            EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN   ORFNames=ADL05_29085 {ECO:0000313|EMBL:KOX07300.1};
OS   Nocardiopsis sp. NRRL B-16309.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX07300.1, ECO:0000313|Proteomes:UP000037694};
RN   [1] {ECO:0000313|Proteomes:UP000037694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutaryl-CoA + 2 H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:13389, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:57378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036548};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC       {ECO:0000256|ARBA:ARBA00037899}.
CC   -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC       {ECO:0000256|ARBA:ARBA00037927}.
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:KOX07300.1}.
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DR   EMBL; LGEC01000148; KOX07300.1; -; Genomic_DNA.
DR   RefSeq; WP_053620198.1; NZ_LGEC01000148.1.
DR   AlphaFoldDB; A0A0N0TJQ5; -.
DR   STRING; 1519494.ADL05_29085; -.
DR   PATRIC; fig|1519494.3.peg.6352; -.
DR   OrthoDB; 5241155at2; -.
DR   Proteomes; UP000037694; 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; PTHR42807; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42807:SF1; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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.
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:UP000037694}.
FT   DOMAIN          24..137
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          141..231
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          243..390
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   397 AA;  42321 MW;  63E4FAB55FE4A4D2 CRC64;
     MSDSQHRPAA PDPRDFLAVD ATLSDTERDV RDAVRAFATR ELLPNVADWF DAGTLPDPRG
     LAKAFGDLGV LGMHLEGYGC GGSSAVAYGL ACRELEAVDS GLRSFVSVQG SLAMAAIHKY
     GSEEHKREWL PRMAAGEAIG CFGLTEPDSG SDPGSMRTRA RRDGSDWVLN GTKMWITNGS
     VADVAVVWAA TDDGIRGFVV PTDTPGFSAN VIHRKLSLRA SITAELVLED VRLPGDAVLP
     LSKGLGSPLS CLNEARYGIV WGAAGAARAC YEAALEYGLT REQFGRPIAG FQLTQRKLAD
     MVVDVNHANM TALRIGRLKD AGECHHNHVS FGKFSCVAAA QRVAAAARSV HGANGITLEY
     PVMRHMVNLE TVATYEGTEE IHALSIGQAV TGLSAFR
//
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