ID A0A160DX12_9GAMM Unreviewed; 390 AA.
AC A0A160DX12;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN ORFNames=I596_3228 {ECO:0000313|EMBL:ANB19217.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB19217.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB19217.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB19217.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) 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}.
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DR EMBL; CP015249; ANB19217.1; -; Genomic_DNA.
DR RefSeq; WP_067649782.1; NZ_CP015249.1.
DR AlphaFoldDB; A0A160DX12; -.
DR STRING; 1300342.I596_3228; -.
DR KEGG; dko:I596_3228; -.
DR PATRIC; fig|1300342.3.peg.3153; -.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000076830; Chromosome.
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.
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:UP000076830}.
FT DOMAIN 19..131
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 135..225
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 237..384
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 390 AA; 42648 MW; 5038B9AF9BE7F35E CRC64;
MATSPLNPTD LYDVRSLLSE EERMVQDTVA RFTDERVLPI IGDCFDRGRF PTELIPEMAE
LGLLGSSLPV EYGCAGMNGV SYGLVCQELE RGDSGLRSFA SVQSSLCMYP IYAYGSEEQR
RRWLPDMAAG KVIGCFGLTE PQGGSDPGSM RTHAKKDGAD WILNGSKMWI TNGNLAHIAI
VWAQTDEGIQ GFVVEKDFPG YAAQEIHKKM SLRASVTSAL YFDNVRVPDA NRLPNVKGLK
GPLGCLTQAR YGITWGPIGA AIACLAEVLD YSKSRILFKQ PIAARQAVQI KLAEMARRIT
LAQLLSLQLG RLKDAGVMQP TQVSLAKWNN CRMAIDIARE ARDILGGAGI TTEHSPIRHA
LNLESVITYE GTETVHQLVV GRELTGINAF
//
