ID V4HEV3_9EURY Unreviewed; 395 AA.
AC V4HEV3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=glutaryl-CoA dehydrogenase (ETF) {ECO:0000256|ARBA:ARBA00039033};
DE EC=1.3.8.6 {ECO:0000256|ARBA:ARBA00039033};
GN ORFNames=K933_08033 {ECO:0000313|EMBL:ESP88648.1};
OS Candidatus Halobonum tyrrellensis G22.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobonum.
OX NCBI_TaxID=1324957 {ECO:0000313|EMBL:ESP88648.1, ECO:0000313|Proteomes:UP000017840};
RN [1] {ECO:0000313|EMBL:ESP88648.1, ECO:0000313|Proteomes:UP000017840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:ESP88648.1,
RC ECO:0000313|Proteomes:UP000017840};
RX PubMed=24336364;
RA Ugalde J.A., Narasingarao P., Kuo S., Podell S., Allen E.E.;
RT "Draft Genome Sequence of 'Candidatus Halobonum tyrrellensis' Strain G22,
RT Isolated from the Hypersaline Waters of Lake Tyrrell, Australia.";
RL Genome Announc. 1:e01001-13(2013).
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:ESP88648.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASGZ01000027; ESP88648.1; -; Genomic_DNA.
DR RefSeq; WP_023394192.1; NZ_ASGZ01000027.1.
DR AlphaFoldDB; V4HEV3; -.
DR STRING; 1324957.K933_08033; -.
DR PATRIC; fig|1324957.4.peg.1629; -.
DR eggNOG; arCOG01707; Archaea.
DR OrthoDB; 275197at2157; -.
DR Proteomes; UP000017840; 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 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:UP000017840}.
FT DOMAIN 12..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..229
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..387
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 395 AA; 42902 MW; 01802DF9BDC6FEF6 CRC64;
MLDYVGLEAD LTEEERLIRD TAREFVEREV EPDIGDHFEA GTFPTDLVAE MGELGFYAPN
LEGYGSPNVS ERAYGILMQE LEAGDSGIRS MASVQGALVM YPIHAFGSEA QKEAWLPALG
RGEAVGCFGL TEPGHGSNPS GMETEARRDG DEFVLNGSKT WITNSPIADV AVVWARLVDD
GGDADGGSED APVRGFLVET DRDGVTTAEI HDKLSMRASV TGEIGLSDVR VPESNLLPGV
EGMKGPLSCL TQARYGIAWG AVGAARDCFE TAREYQLDRD QFGGPVARFQ IQQEKLAEMA
TQVTTAQLLA YRLAALKEEG RLRPQQVSMA KRNNVRTARD QARVAREMLG GNGITTDYSP
MRHMANMETV YTYEGTHDIH SLILGEDLTG IAAFE
//
