ID A0A0W1R9X9_9EURY Unreviewed; 380 AA.
AC A0A0W1R9X9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KTG10329.1};
GN ORFNames=AUR64_12205 {ECO:0000313|EMBL:KTG10329.1};
OS Haloprofundus marisrubri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloprofundus.
OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG10329.1, ECO:0000313|Proteomes:UP000054387};
RN [1] {ECO:0000313|EMBL:KTG10329.1, ECO:0000313|Proteomes:UP000054387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB9 {ECO:0000313|EMBL:KTG10329.1,
RC ECO:0000313|Proteomes:UP000054387};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT archaeon isolated from the Discovery deep brine-seawater interface in the
RT Red Sea.";
RL Submitted (DEC-2015) 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:KTG10329.1}.
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DR EMBL; LOPU01000018; KTG10329.1; -; Genomic_DNA.
DR RefSeq; WP_058581683.1; NZ_LOPU01000018.1.
DR AlphaFoldDB; A0A0W1R9X9; -.
DR STRING; 1514971.AUR64_12205; -.
DR OrthoDB; 275197at2157; -.
DR Proteomes; UP000054387; 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; cd01158; SCAD_SBCAD; 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; 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; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 380 AA; 41455 MW; 4A0291269C71D10F CRC64;
MDFQLSAEQK QIRDMVAEFV DEEIRPVAAD IDENDEFPAD LVSEMAELGL MGMPFPEEYG
GAGLDYHSYA IGLEEISRGS GGLGTVVAAH ISLAGNMVYA FGDEEQKQEY LTPVNTGEDI
GAFALSEAGA GSDVPSMTTT AEKDGDEYVV NGGKLWISNG SVADTVTLFA KTDPDAGNKG
ISSFIVRPEE DDGFVVEGTE HKLGDKGCPT AELRFDDMRI PEDRLLGEEG DGFVHALKTL
NGGRITIAAR SIGIARAARD DALQYAQERE QFDQQIARFQ SIQHKLADMD TKIQAAKLLM
HQAADKKIRG ENFIKEAAQA KLYASEISRE VANEGIQIHG GYGYTKDFAA ERYYRDAKLN
EIYEGTSEIL RNTIAAQLLD
//
