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Database: UniProt
Entry: A0A2T9Z8I6_9FUNG
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ID   A0A2T9Z8I6_9FUNG        Unreviewed;       425 AA.
AC   A0A2T9Z8I6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE            EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN   ORFNames=BB560_004712 {ECO:0000313|EMBL:PVV00890.1};
OS   Smittium megazygosporum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133381 {ECO:0000313|EMBL:PVV00890.1, ECO:0000313|Proteomes:UP000245609};
RN   [1] {ECO:0000313|EMBL:PVV00890.1, ECO:0000313|Proteomes:UP000245609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-DP-2 {ECO:0000313|EMBL:PVV00890.1,
RC   ECO:0000313|Proteomes:UP000245609};
RX   PubMed=29764946;
RA   Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT   "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT   Symbiosis.";
RL   MBio 9:e00636-e00618(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutaryl-CoA + 2 H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:13389, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:57378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036548};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC       {ECO:0000256|ARBA:ARBA00037899}.
CC   -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC       {ECO:0000256|ARBA:ARBA00037927}.
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:PVV00890.1}.
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DR   EMBL; MBFS01001536; PVV00890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T9Z8I6; -.
DR   STRING; 133381.A0A2T9Z8I6; -.
DR   Proteomes; UP000245609; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000245609}.
FT   DOMAIN          47..158
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          162..255
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          268..414
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   425 AA;  46655 MW;  77310993BDA09866 CRC64;
     MLKSNLRLLQ VSKQLVNSSK RFYASGSGSG MVKYNWEDPF DFRSQLSEEE QIVSDAVRSY
     CQEKLLPRVH DNFRNETHDK RIFEEMGELG LLGSTINGYG CAGTNYVTYG LTAHEVEAVD
     SGYRSGMSVQ SSLVMHPINA FGSEDQKQRY LPGLAKGKLV GAFGLTEPNH GSDPGSMETT
     AKKSGKIYTL NGSKTWITNS PIADVFVVWA KNQDENGAIR GFILEKDMKG LSAPKINGKF
     SLRASPTGMI LMDDVQVPEE NMLPNVKGLK GPFSCLNNAR FGIAWGALGA ARSCLHTARQ
     YTIDRKQFGV PLASNQLIQY KLADAHSEIA IGLQACLRVG RLKDEGRWAP EMVSVIKRNS
     AQKALNIARQ CRDMLGGNGV SDEYNVIRHM VNLEAVNTYE GTHDVHSLIL GRAITGIPSF
     VAKGQ
//
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