ID I0KVL5_9ACTN Unreviewed; 386 AA.
AC I0KVL5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:CCH15612.1};
DE EC=1.3.99.7 {ECO:0000313|EMBL:CCH15612.1};
GN Name=GCDH {ECO:0000313|EMBL:CCH15612.1};
GN ORFNames=MILUP08_40520 {ECO:0000313|EMBL:CCH15612.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH15612.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
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:CCH15612.1}.
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DR EMBL; CAIE01000006; CCH15612.1; -; Genomic_DNA.
DR RefSeq; WP_007454852.1; NZ_HF570108.1.
DR AlphaFoldDB; I0KVL5; -.
DR STRING; 1150864.MILUP08_40520; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 3176804at2; -.
DR Proteomes; UP000003448; 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 ECO:0000313|EMBL:CCH15612.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448}.
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 233..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 41479 MW; 6DB209C1B7788CE8 CRC64;
MTALDLLDLD PSLSAEERQI RDVVRQLVDD RVRPHVAAWY EEGRVPAREL AREFGKLGLL
GMHLTGYGCA GASAVAYGLA CQELEAGDSG LRSLVSVQGS LAMYAIWRYG SEEQKQRWLP
AMATGEAIGC FGLTEPDHGS DPASMTTRAR RDGDDWILAG AKMWITNAPI ADVAVIWART
DEGVRGFAVP MDTPGVTARE IGRKMSLRAS VTGEIALDDV RLPADAQLPD AIGLKAPLSC
LTEARYGIVW GSLGAARDCL ETALAYATSR TQFGRPLAGF QLTQAKLADM AVELVKGQLL
ALHLGRLADA GRLRPEQVSV GKLNNVREAL AIARQCRTIL GANGVSGEYP VMRHANNLES
VLTYEGTSEI HQLVVGQRLT GLSAFA
//
