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Database: UniProt
Entry: A0A1B1ZKK9_9PSEU
LinkDB: A0A1B1ZKK9_9PSEU
Original site: A0A1B1ZKK9_9PSEU 
ID   A0A1B1ZKK9_9PSEU        Unreviewed;       398 AA.
AC   A0A1B1ZKK9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ANY06293.1};
GN   ORFNames=AFB00_08280 {ECO:0000313|EMBL:ANY06293.1};
OS   Pseudonocardia sp. HH130630-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1690815 {ECO:0000313|EMBL:ANY06293.1, ECO:0000313|Proteomes:UP000092926};
RN   [1] {ECO:0000313|EMBL:ANY06293.1, ECO:0000313|Proteomes:UP000092926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130630-07 {ECO:0000313|EMBL:ANY06293.1,
RC   ECO:0000313|Proteomes:UP000092926};
RA   Oliw E.H.;
RL   Submitted (JAN-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; CP013854; ANY06293.1; -; Genomic_DNA.
DR   RefSeq; WP_068796744.1; NZ_CP013854.1.
DR   AlphaFoldDB; A0A1B1ZKK9; -.
DR   STRING; 1690815.AFB00_08280; -.
DR   KEGG; phh:AFB00_08280; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000092926; 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   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; 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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092926}.
FT   DOMAIN          25..134
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          140..232
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          252..390
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   398 AA;  43787 MW;  405C85A2779AA8B3 CRC64;
     MSTTPYTELG EALGTDFFSV RDQFTDEQWQ RFTDVRRFVD TEVLTDINDY WERAELPWHL
     FRRLPGLGIV GEDIQGYGAA AMSPLALGLV HMELHRGDGS LGTFLGVHAG LAMKAIDMCG
     SDEQRARWLP SMSALERTGA FALTEPDHGS DSVALETTAT RDGDHWILRG TKRWIGNGTV
     ADLVVVWARD TDSGDVLGFV VETPAEGYSA TVIPGKVSLR ALWQADITLD RVRVPDENRL
     AKARTFADCA AVLATTRSTC AWMALGHATA GYEAALRYAT EREQFGRPLA SFQIVQERLV
     RMLADLTGMQ LYCMQTARLA EAGKLSPTVA GLAKMHNTRT ARSILSEARD LLGGNGILLE
     HHVVRHWADI EAIHTFEGTE TMQTLIVGRD VTGFSAFT
//
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