ID M5BYS0_THACB Unreviewed; 636 AA.
AC M5BYS0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:CCO31745.1};
DE EC=1.3.8.6 {ECO:0000313|EMBL:CCO31745.1};
GN Name=GCDH {ECO:0000313|EMBL:CCO31745.1};
GN ORFNames=BN14_05795 {ECO:0000313|EMBL:CCO31745.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO31745.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO31745.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
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:CCO31745.1}.
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DR EMBL; CAOJ01008711; CCO31745.1; -; Genomic_DNA.
DR AlphaFoldDB; M5BYS0; -.
DR HOGENOM; CLU_430323_0_0_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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 InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CCO31745.1}.
FT DOMAIN 429..540
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 544..609
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT REGION 308..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 68979 MW; 8348AF4CF041828C CRC64;
MRKATGDYMF DLTWHHSNFE IALGGCRFTC APQISILVHV NNEDGFHLGA HQLESTLAAK
AKGATDSTIL FKMMASETAI SASPAGNTHS SGQSTRRRLS PQLRVDIANS LNEPGIISQS
DTPSAGVWYR PGLPEEDIPL NLGAERSWDG AKGISVAQGR QRSNTVVGAT FASLGTSPRS
MTGLGFYTGD AEAPLQPALN SDGTSSAYGY DVPMGSEFDD ELTRRLLREK RQLTEEGRWI
DDGDIGSIVS RRAVPDEQTE AAPNLLCNIC IFAAPYTLKH WNWPTGRPTA PTLADDERLS
TLDIRRESSA KLPQPIPQGS HTQKTLVSAS LPQNEGPHPK SIKQRGTDHM RNDKASQLPS
PPITPAILPI SLYEQRTISF SEKAQRSSDR ETPIGLVASI EKIVGEQFSR ALSILALGLD
PLNLDALLTE EERAIRDTAR DYCQENLQPR VLEAYRNEDF DPRILSEMGK LGLLGATIKG
YGCAGVSSVA YGLIAREVER VDSGYRSAMS VQSSLVMHPI NAYGSKEQKE KYIPQLASGE
LVGCFGLTEP NHGSDPSSME TTADQDASTG GYTLNGSKTW ISNAPVAGLF VVWARCLWDK
KIRGFLIEKR LVTAFRGPSS IADDQVSSAH HSAGAI
//
