ID A0A345DZE6_9EURY Unreviewed; 386 AA.
AC A0A345DZE6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN ORFNames=DU500_02120 {ECO:0000313|EMBL:AXG05318.1};
OS Haloplanus rubicundus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloplanus.
OX NCBI_TaxID=1547898 {ECO:0000313|EMBL:AXG05318.1, ECO:0000313|Proteomes:UP000253273};
RN [1] {ECO:0000313|EMBL:AXG05318.1, ECO:0000313|Proteomes:UP000253273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1113 {ECO:0000313|EMBL:AXG05318.1,
RC ECO:0000313|Proteomes:UP000253273};
RA Kim Y.B., Roh S.W.;
RT "Genome sequences of Haloplanus sp. CBA1113.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP031150; AXG05318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345DZE6; -.
DR KEGG; haj:DU500_02120; -.
DR OrthoDB; 275197at2157; -.
DR Proteomes; UP000253273; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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}.
FT DOMAIN 13..122
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..378
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 42426 MW; ED63D344191066CB CRC64;
MLDYVDLEAD LGEEERLIRD TARRFVDEQV RPDIGDHFLD GTFPTDLIPE MGELGFYGSN
LDGYGLPNVS ERAYGLLMQE LEAGDSGVRS MASVQGALVM YPIHRFGTEG QKERWLPELA
TGAAVGCFGL TEPEHGSDPS SMATRATRDG DGYRLTGSKT WITNAPIADV AVVWARDRSD
PDDPVRGFLV ETERDGVRTP KIDEKLSLRA SITGEISLSD AWVPAENVLD VTGMKGPLSC
LTQARYGIAW GAVGAARDCF ETAREYATER EQFGKPIGGF QLQQEKLAEL ATRVTTGQLL
AHRLADLKER GELRPQQVSM AKRNNVRMAR EGSRVAREIL GGNGITADYP PMRHLANMET
VYTYEGTHDI HSLILGEDLT GLSAFE
//
