ID A0A1I5RG50_9ACTN Unreviewed; 391 AA.
AC A0A1I5RG50;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:SFP57518.1};
GN ORFNames=SAMN05660464_3529 {ECO:0000313|EMBL:SFP57518.1};
OS Geodermatophilus dictyosporus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1523247 {ECO:0000313|EMBL:SFP57518.1, ECO:0000313|Proteomes:UP000198857};
RN [1] {ECO:0000313|Proteomes:UP000198857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44208 {ECO:0000313|Proteomes:UP000198857};
RA Varghese N., Submissions S.;
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; FOWQ01000006; SFP57518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5RG50; -.
DR STRING; 1523247.SAMN05660464_3529; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000198857; 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; 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:UP000198857}.
FT DOMAIN 25..126
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 132..225
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 240..384
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 391 AA; 43130 MW; 30D91F91FB59B574 CRC64;
MTDELPGDLY DYESLLSEDE RKELLGIRRF LHEEVRPRVN QSWETATFPM DLIPRFAEEG
MVGRSYDLEH RPRASRLFTG FISLEASRVD PSMATFLGVH NGLSMGSIVL LGSDEQRARW
VPDMVSLQRI GAFALTEPHG GSDVAQGLET TCRRDGDEWV IDGAKRWIGN GTFADVVVVF
ARDVADDQVK TLVVEKGTPG FTATKMEGKY ALRTVQNADI VFEDCRVPAE NKLAEGNSFR
DVNRVLKLTR GGVAWNAVGC QMGAFEAAIA YAKDRRQFGR QIAGFQLIQD LLARMAGNVT
ASLGMAVRVS QLQEEGVFRD EQAALAKAFV TGRARETVAL ARELFGGNGI LLENDVVRYF
ADAEALYSYE GTREINSLIV GRALTGVSAF V
//
