ID A0A1Q3E043_LENED Unreviewed; 429 AA.
AC A0A1Q3E043;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutaryl-dehydrogenase {ECO:0000313|EMBL:GAW00560.1};
GN ORFNames=LENED_002088 {ECO:0000313|EMBL:GAW00560.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW00560.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAW00560.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW00560.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAW00560.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW00560.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) 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:GAW00560.1}.
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DR EMBL; BDGU01000032; GAW00560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3E043; -.
DR STRING; 5353.A0A1Q3E043; -.
DR Proteomes; UP000188533; 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 CDD; cd01151; GCD; 1.
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}.
FT DOMAIN 53..161
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 170..262
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 274..421
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 429 AA; 46443 MW; 745786BE3658C16A CRC64;
MFGISRRTLC KSIASRNAER AVPSLVRCAS TASGSKFAKF DWEDPLNMDS LLTEEEKAIR
DSANAYCQEK LMPRVLHGWR TEEFDPAVIP EMGAIGLLGP TIQGYGCAGV SNVAYGLIAR
EIERVDSGYR STASVQSSLV MHPIYEFGSE AQKEKYLPRL VVARGEIIGA FGLTEPNHGS
DPAGMETTAE DIDGGFIING SKTWISNAPV ADVHVIWARC KWDNKIRGFL LEKGTQGLSA
PPIKNKVSLR VSLTGSIFMD NVRVPQDSLL PGTKGLGSAF SCLNSARYGI SWGVMGALED
CVARARSYAL ERHQFQRPIA SFQLIQKKLA EAQSEVAIGL LASLQVGRLK DQGLLAPEMV
SLVKKNNCGK ALHHARSVLD ILGGNAASDE YHIARHASNL QITNTYEGTN DVHALILGKA
ITGIQAFAN
//
