ID A0A369JRX7_HYPMA Unreviewed; 421 AA.
AC A0A369JRX7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 12.
DE SubName: Full=Glutaryl-CoA dehydrogenase, mitochondrial {ECO:0000313|EMBL:RDB25031.1};
GN Name=GCDH {ECO:0000313|EMBL:RDB25031.1};
GN ORFNames=Hypma_007612 {ECO:0000313|EMBL:RDB25031.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB25031.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB25031.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB25031.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-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:RDB25031.1}.
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DR EMBL; LUEZ02000041; RDB25031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JRX7; -.
DR STRING; 39966.A0A369JRX7; -.
DR InParanoid; A0A369JRX7; -.
DR Proteomes; UP000076154; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076154}.
FT DOMAIN 47..158
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..254
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 266..413
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 421 AA; 45668 MW; E34C29091B706900 CRC64;
MLRLSRAAPS RVLQTTLKTS VSSQRAASTQ LAKFQWEDPL NLESLLTEEE IAIRDTAQNY
CQEKLLPRVL EGWRTEEFNH SIIPEMGALG LLGPTISGYG CAGVSNVAYG LIAREIERVD
SGYRSTASVQ SSLVMHPIDE FGTEAQKEKY LPRLAKGEII GAFGLTEPNH GSDPAGMETT
AEEVDGGFII NGSKTWISNA PVADIFVIWA NCKWDNKVRG FVLEKGLKGL SAPPIKNKIA
LRASLTGSIF MDSVKVSHDA LLPKTRGLGS AFSCLNSARF GISWGVMGAL EDCVHRTRAY
ALERHQFKRP LASFQLVQKK LVDAQTEVAL GLLASLQVGR LKDAGKVAPE MISLVKRNNC
GKALQQARIV LDILGGNAAS DEYHVGRHVA NLQVTNTYEG TNDIHALILG KAITGIQAFA
N
//
