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Database: UniProt
Entry: A0A1G9UXF0_9EURY
LinkDB: A0A1G9UXF0_9EURY
Original site: A0A1G9UXF0_9EURY 
ID   A0A1G9UXF0_9EURY        Unreviewed;       379 AA.
AC   A0A1G9UXF0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SDM64476.1};
GN   ORFNames=SAMN05192554_10557 {ECO:0000313|EMBL:SDM64476.1};
OS   Haloarchaeobius iranensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halorubellaceae; Haloarchaeobius.
OX   NCBI_TaxID=996166 {ECO:0000313|EMBL:SDM64476.1, ECO:0000313|Proteomes:UP000199370};
RN   [1] {ECO:0000313|EMBL:SDM64476.1, ECO:0000313|Proteomes:UP000199370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC   {ECO:0000313|Proteomes:UP000199370};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNIA01000005; SDM64476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9UXF0; -.
DR   STRING; 996166.SAMN05192554_10557; -.
DR   OrthoDB; 275197at2157; -.
DR   Proteomes; UP000199370; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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   PIRSF; PIRSF016578; HsaA; 2.
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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199370}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..216
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          228..379
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  41009 MW;  E44A978BC54C32BB CRC64;
     MSFQLSDEQR AIRDAVREFG ANEIRPVARE HDEAKQYPHD LVQEAAEYDL VAPTIDPEYG
     GAGMDLLESV VVTEELWRAD PGIGSAIGSR GFGSTMIQEF GDDWMKAEWL PRVASGESAT
     CSCISEPAHG SNVAGIETRA ERDGDEWALN GTKMWITNGT VADVAVVMAK TDPDAGHRGI
     TAFLVPTDLD GFETTKIDNK LGIRASDLAE IVLDDVRVPA ENVIGEVGKG FYQLMAFFAD
     GRTNVAAQAI GTAQAALDAA VDYAAEREQG GQRIGEYQAI RHKLSEMATN VEAARSLAYR
     AATHVEDGDD DVAAKFASMA KLFASEHAVD VADEAIQVHG GAGFVTDHPV ERFYRDARIT
     KIYEGTSEIQ KNIIADRLL
//
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