ID A0A1H6ZG53_9BACT Unreviewed; 452 AA.
AC A0A1H6ZG53;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:SEJ48520.1};
GN ORFNames=SAMN05216327_11193 {ECO:0000313|EMBL:SEJ48520.1};
OS Dyadobacter sp. SG02.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1855291 {ECO:0000313|EMBL:SEJ48520.1, ECO:0000313|Proteomes:UP000199631};
RN [1] {ECO:0000313|EMBL:SEJ48520.1, ECO:0000313|Proteomes:UP000199631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG02 {ECO:0000313|EMBL:SEJ48520.1,
RC ECO:0000313|Proteomes:UP000199631};
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; FNYL01000011; SEJ48520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ZG53; -.
DR STRING; 1855291.SAMN05216327_11193; -.
DR OrthoDB; 9764422at2; -.
DR Proteomes; UP000199631; 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}.
FT DOMAIN 78..189
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 193..286
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 305..445
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 452 AA; 50204 MW; 275CD2A98C158AFB CRC64;
MNLFKSISQL RNLLKTIDIE AVARLSQKVD LNKLMGIVSK MSEEDLGKML KFMQAGSGKK
KAPPVVNGDF YELASTLTPE DREIQLKVRE FMETEIKPIA NYYWNNAQFP KHIIPLMAKL
DICGLTYQGY GCAGRSALLE GFIAMEMARI DSSVSTFFGV HSGLAMGSIY LCGSEEQKQQ
WLPVMQRMEL IGAFGLTEPE VGSGAAGGLT TTCKREGDEW VINGQKKWIG NATFSDITII
WARDLDDNQV KGFIVRKENP GFKAEKMEDK MALRTVQNAL ITLTDCRVPE ADRLQNANSF
KDTANVLRMT RAGVAWQAVG CGRGAYELAL KYTMERRQFG RPIAGFQLVQ DLLVTMLGDL
TAMQTMVYRL SQLQDAGDLA DEHASLAKVF CTLRMRSIVD HARELFGGNG ILLEYDIARF
VADAEAIYSY EGTKEINSLI VGRAITGESA FV
//
