ID A0A075R0E4_BRELA Unreviewed; 568 AA.
AC A0A075R0E4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:AIG24668.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:AIG24668.1};
GN ORFNames=BRLA_c002730 {ECO:0000313|EMBL:AIG24668.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG24668.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG24668.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG24668.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
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; CP007806; AIG24668.1; -; Genomic_DNA.
DR RefSeq; WP_003333698.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075R0E4; -.
DR STRING; 1042163.BRLA_c002730; -.
DR KEGG; blr:BRLA_c002730; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_3_9; -.
DR Proteomes; UP000005850; Chromosome.
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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
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; PF21263; Acyl-CoA-dh_C; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850}.
FT DOMAIN 30..141
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 145..237
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 249..409
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 446..531
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 568 AA; 63071 MW; 5CAD4FA93685EA49 CRC64;
MGIREDNKCL VVGSCLFDNQ SFFSPEDFEA EEELIAKTTE QFVQSAIIPK LERIEQHDYS
VTRKLFTQAG ELGLLGVDVP EAYGGVSLGK KVSGLVAEKM GYAGSFSISF NIHAGVGTLP
YVYYGTEEQK QRILPKLVSG EWIAGYALTE PNAGSDALQA RTSAYLNDAG TAWILNGEKQ
WITNARIADV FVVFAKTQLG MTAFIVEKSA SGVSLGPEEK KMGIKGSSTA TLLLEEVSIP
VTNVLGEVGK GHRVALNILN LARLKLAFGN IGTAKQALQL SIAYGTTRQQ FGKKLVEFPM
IQEKIANMAV AIYASESAAY RTAGVIDDFL HSKEEASNEL SKYAMECAIN KVASSEALAW
IVDEAVQIHG GYGYMQDYEV ERLYRDARIS RIFEGTNEIN RLTIARALLK RTIAKEEIRM
HDELSRNQQF LYYAKQLLYD ALEMLAKRIN QQVEQEQEYL RLLADSIRDI YMMESVLIRN
QKARAKHGAD KEEVKQLMTD VLCEEGYRQV EAATISIISS LESKETSRRA LVDSIRSKTL
SMYSNLVLAK RKIANKMIIS GKYVVEGG
//
