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Database: UniProt
Entry: A0A0L1LMR6_9MICC
LinkDB: A0A0L1LMR6_9MICC
Original site: A0A0L1LMR6_9MICC 
ID   A0A0L1LMR6_9MICC        Unreviewed;       396 AA.
AC   A0A0L1LMR6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KNH17492.1};
GN   ORFNames=ACU18_10320 {ECO:0000313|EMBL:KNH17492.1};
OS   Arthrobacter sp. ZBG10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1676590 {ECO:0000313|EMBL:KNH17492.1, ECO:0000313|Proteomes:UP000036861};
RN   [1] {ECO:0000313|EMBL:KNH17492.1, ECO:0000313|Proteomes:UP000036861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZBG10 {ECO:0000313|EMBL:KNH17492.1,
RC   ECO:0000313|Proteomes:UP000036861};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-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:KNH17492.1}.
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DR   EMBL; LFQH01000039; KNH17492.1; -; Genomic_DNA.
DR   RefSeq; WP_050685456.1; NZ_LFQH01000039.1.
DR   AlphaFoldDB; A0A0L1LMR6; -.
DR   PATRIC; fig|1676590.3.peg.1899; -.
DR   Proteomes; UP000036861; 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   GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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; PS00072; ACYL_COA_DH_1; 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}.
FT   DOMAIN          27..131
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          137..230
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          245..389
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   396 AA;  43154 MW;  726216A4442DE5E0 CRC64;
     MSATPAGLNT LPYADGDFFA FEQLLTQKEQ DRLAEIRDFL AREVKPIAVD CWNRGEFPMD
     LIPKLAEIDL ISPVRRQGHS NLFAGLVHAE LTRADASIAT FLGVHDGLFT GSIEALASQE
     QKDAWLPDIY AMKKIGAFGL TEPLGGSDVA GGTRTTARRD GDSWILNGEK RWIGNATFSD
     WVVIYARDLD DNKVKGFLVD TSLPGYSATK IENKISLRTV QNADITLTNV VVPDFFKLAH
     ANSFRDVNKV LKVTRLGVAW QAVGQQLAAF DVARSYAVER QQFGRPLASF QLVQSQLVSI
     LGNAVSSMGM MVRLSQLEDA GQAKDEQSAL AKAFTTERMR DSVAIGRNIL GGNGIVTDYG
     MAKIFADAEA IYSYEGTHEI NTLVTGRAVT GISAIV
//
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