ID A0A1C6S6W6_9ACTN Unreviewed; 386 AA.
AC A0A1C6S6W6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:SCL25016.1};
GN ORFNames=GA0070616_3028 {ECO:0000313|EMBL:SCL25016.1};
OS Micromonospora nigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL25016.1, ECO:0000313|Proteomes:UP000199699};
RN [1] {ECO:0000313|EMBL:SCL25016.1, ECO:0000313|Proteomes:UP000199699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL25016.1,
RC ECO:0000313|Proteomes:UP000199699};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMHT01000003; SCL25016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6S6W6; -.
DR STRING; 145857.GA0070616_3028; -.
DR OrthoDB; 3176804at2; -.
DR Proteomes; UP000199699; 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:UP000199699}.
FT DOMAIN 14..126
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 130..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 232..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 41551 MW; E721FBDCCE193537 CRC64;
MSPVDLLDLD SSLSEEERQV RAVVRRLVDD RVRPHVAGWY EDGQVPARDL AREFGKLGLL
GMHLTGYGCA GSSAVAYGLA CLELEAGDSG VRSLVSVQGS LAMYAVWRYG SEEQKQRWLP
AMATGEAIGC FGLTEPDHGS DPASMATRAR RDGDDWVLTG SKMWITNAPI ADVAVIWART
DEGVCGFAVP MDTPGVTARE IRRKMSLRAS VTGEISLDDV RLPADARLPE ATGLKAPLSC
LTEARHGIVW GALGAARDCL ETTLGYAATR TQFGRPLAGF QLTQAKLADM AVEWTKGYLL
AVQLGRLADA GRLRPDQVSV GKLNNVREAL AIARQCRTIL GANGVSGDYP VMRHANNLES
VLTYEGTSEI HQLVIGQRLT GLSAFV
//
