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Database: UniProt
Entry: A0A0H2KU01_9MICO
LinkDB: A0A0H2KU01_9MICO
Original site: A0A0H2KU01_9MICO 
ID   A0A0H2KU01_9MICO        Unreviewed;       413 AA.
AC   A0A0H2KU01;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KLN35354.1};
GN   ORFNames=FB00_08010 {ECO:0000313|EMBL:KLN35354.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35354.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN35354.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN35354.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) 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:KLN35354.1}.
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DR   EMBL; JNBQ01000005; KLN35354.1; -; Genomic_DNA.
DR   RefSeq; WP_047232318.1; NZ_JNBQ01000005.1.
DR   AlphaFoldDB; A0A0H2KU01; -.
DR   STRING; 264251.FB00_08010; -.
DR   PATRIC; fig|264251.5.peg.1630; -.
DR   Proteomes; UP000035265; 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; 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.
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:UP000035265}.
FT   DOMAIN          33..144
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          148..247
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          268..406
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   413 AA;  44394 MW;  F3DFD7FEF497B8CC CRC64;
     MPTTPIMPGV TEPTYDLATP LDLDYAGAFA DATEEDRAHQ QRVRQFVQDE VLPVIDDYWE
     RAEVPFDLVK RMGELDLLRD GVDVEGRPRV SLLGAGLAAM EMSRGDGSVA TICGVQGGLA
     LRSIQMLGSD EQRAKYAEPM ARGEILGAFA LTEPTHGSDS VSLETTARKE TRDGVEGYVL
     NGEKKWIGNG SSGHITVVWA RLVGDGGDNQ VHGFVVPQDT PGYTGTTITG KVSLRAIWQA
     HVVLDDVFVP AENALPGARS FKDTSRVLFA TRLGVAWAAV GHAVACYEAA VAYAKQRVQF
     GRPLAANQMV QERLTKMLST ITQLQLLVAQ MTRLDEAGTL TGPQASLAKY TCTRGAREVA
     ASARDLLGGN GILLQNRVAR HFADVEALHT YEGTESVQAL IVGRDITGVS AFV
//
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