ID A0A3R9PT24_9BACT Unreviewed; 397 AA.
AC A0A3R9PT24;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:RSL17292.1};
GN ORFNames=EDE15_2822 {ECO:0000313|EMBL:RSL17292.1};
OS Edaphobacter aggregans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Edaphobacter.
OX NCBI_TaxID=570835 {ECO:0000313|EMBL:RSL17292.1, ECO:0000313|Proteomes:UP000269669};
RN [1] {ECO:0000313|EMBL:RSL17292.1, ECO:0000313|Proteomes:UP000269669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB153 {ECO:0000313|EMBL:RSL17292.1,
RC ECO:0000313|Proteomes:UP000269669};
RA Deangelis K.;
RT "Sequencing of bacterial isolates from soil warming experiment in Harvard
RT Forest, Massachusetts, USA.";
RL Submitted (DEC-2018) 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}.
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:RSL17292.1}.
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DR EMBL; RSDW01000001; RSL17292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9PT24; -.
DR OrthoDB; 105706at2; -.
DR Proteomes; UP000269669; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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; 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.
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:UP000269669}.
FT DOMAIN 18..129
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 133..231
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 243..391
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 397 AA; 43990 MW; 872F59FC62ADE94B CRC64;
MAFKFQGVDF IGFDALLSED ELLVRANTRA FIEDKLIPII EQCNRDGRFP KELVRPMGEL
GFYGATLDGY GCAGMNNVEY GLLTQELERG DSGIRSFVSV QSALVMYPIY TFGSDEQKSF
WLPKMTTGEK LGCFGLTEPD FGSNPAGMRT RARQDGDNYI LNGEKMWITS GSLADVAVIW
AKVEEPSVSP DAWRVRGFLV ETDRPGFSAQ DVHGKWSLRA SVTSGLSMQE VRIPAANLLP
KSDGLKSPLM CLSQARYGIS WGAIGAAMAC YDVALQYAKQ RKQFRNQPIA SHQLVQEKLA
WMVTEITKAQ LLSLQVGRLK DQGNAAFQHI SMAKKNNVWM ALECARMARD ILGANGIADD
YPIMRHMMNL ESVKTYEGTH DIHTLILGQS ITGISAF
//
