ID A0A268K3B9_9BACI Unreviewed; 537 AA.
AC A0A268K3B9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PAE41100.1};
GN ORFNames=CHI06_13895 {ECO:0000313|EMBL:PAE41100.1};
OS Bacillus sp. 7884-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021693 {ECO:0000313|EMBL:PAE41100.1, ECO:0000313|Proteomes:UP000216214};
RN [1] {ECO:0000313|EMBL:PAE41100.1, ECO:0000313|Proteomes:UP000216214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7884-1 {ECO:0000313|EMBL:PAE41100.1,
RC ECO:0000313|Proteomes:UP000216214};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {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:PAE41100.1}.
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DR EMBL; NPDD01000112; PAE41100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268K3B9; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000216214; 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; 2.40.110.20; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 1.
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:UP000216214}.
FT DOMAIN 25..156
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 185..281
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 292..461
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 537 AA; 60762 MW; 7DBDBF61D6F5214B CRC64;
MSLTSHETET RGKNTYSFDE FVTRRQSLDW YRDEPFLQKV VKKYTEAQFE QVHEKILTFS
PRVSSKWNTL AERNARPEAR PYMLHYDAFN HRIDRIVRPL EVHQLEYEVF GEGLFSSKMP
PWESFVKRML THQIGEGGVT CPLTCTHGLI ALLDQFPNNE IPELHEILLH TKEGINGEFA
IGAQFMSEIQ GGSDLPANVL EAVPDGRNYR LHGNKFFCSA AHAEYSVVTA KITGTNKVST
FIVPAWLPGD KEKEKRNGYE INRIKWKLGT AELPTAEIQY NGALAYPIGP KDKGIAVAVG
IVLTLSRLEI GIACAGFMLR ASREANLYGD FRTVFGKKVK DYPLAASKLK KIENAANRTT
AGAFKIYDLF LRLEKPLNPG IKSDHPIEVR KQLFNLRELV LLQKICATNE GAEVLREAIS
IFAGHGVMEE FSALPRIFRD VVVNEQWEGP RNLLLTQIYR DLQRVADWYS PADFVGNVLG
GAPHETIDKF SNQLEDLLQR PVLGEVSEAS MKAAEEWDTF CDSFFKAFQE TALAEIE
//
