ID A0A1I5FGM9_9PSEU Unreviewed; 394 AA.
AC A0A1I5FGM9;
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:SFO22907.1};
GN ORFNames=SAMN05421805_11160 {ECO:0000313|EMBL:SFO22907.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFO22907.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFO22907.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFO22907.1,
RC ECO:0000313|Proteomes:UP000199398};
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; FOUP01000011; SFO22907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5FGM9; -.
DR STRING; 455193.SAMN05421805_11160; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000199398; 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}.
FT DOMAIN 20..130
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 135..228
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 245..387
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 394 AA; 43101 MW; 0EE29C8A063A2A70 CRC64;
MPKPVNTDPD FFGFADLLSE AERAELAEIR EYLEREIKPL ANDAWEKAEF PFEVVAKFAR
LNLAGYQYPE YGDGTSRSPL FTGFLSLELN RIDPSLAVFS GVHTGLAMGS IYNGGDQEQR
DRWIPDMADM SKIGAFALTE PEGGSDVAGG MRTTARRDGD EWVLNGAKRW IGNGTFADLV
VVWARDEADG QVKGFVVEKG TPGFTASKIE GKIALRTVQN ADIVLTDVRV PEADRLQNIN
SFRDTAKVLA KTRGGVAWQA LGVAVRAYEL AREYAVNRVQ FGKPIAAFQM IQDLLVKMLG
NITAMFGIVV RLNELVAQGR GGAEQAALAK AFTTTKMREV VAWARELFGG NGIVLDYEVA
KFFSDAEAVY SFEGSREMNT LIVGKSITGH SAFA
//
