ID A0A1G9PC24_9BACI Unreviewed; 383 AA.
AC A0A1G9PC24;
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:SDL96308.1};
DE Flags: Fragment;
GN ORFNames=SAMN05443253_101301 {ECO:0000313|EMBL:SDL96308.1};
OS Bacillus sp. OK048.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882761 {ECO:0000313|EMBL:SDL96308.1, ECO:0000313|Proteomes:UP000199133};
RN [1] {ECO:0000313|EMBL:SDL96308.1, ECO:0000313|Proteomes:UP000199133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK048 {ECO:0000313|EMBL:SDL96308.1,
RC ECO:0000313|Proteomes:UP000199133};
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; FNHN01000001; SDL96308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9PC24; -.
DR STRING; 1882761.SAMN05443253_101301; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000199133; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 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; 3.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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:UP000199133}.
FT DOMAIN 1..114
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 118..214
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 228..362
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SDL96308.1"
SQ SEQUENCE 383 AA; 42492 MW; A88330315D98F592 CRC64;
TQEQEMIRKT ARDIASQFDD EYWRKADKEH RFPQEFYDAY ADAGLIGVMI SEEYGGGGLG
VTEAALILHE IAKSPAGFDG ASTIHASLFG PNPLFFHGNK EQKEKYMPSI ANGELQVCFG
VTEPNAGTDT TRITTFAKRE GDKYIINGHK VFITKAQKSE RILLVARTTP YDQVTKKTDG
MSLFFAPNDR SAITIKEIEK MGRNAIDTNE LFIEGLEVDA SDLIGKEGKG FKYLLDGLNP
ERILVAFEAI GIGYSAIERA SKYANERVVF GRPIGKNQGV QFPLADAYSH LKAAEALAYR
AAWLYDNGRP CGPEANMAKL RASEAGFAAV NAAMQTFGGY SYATEYNIER FYRQIHLPRV
APINNEMVKA YVAQHCLGMP RSY
//
