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Database: UniProt
Entry: A0A094PNN9_9ACTN
LinkDB: A0A094PNN9_9ACTN
Original site: A0A094PNN9_9ACTN 
ID   A0A094PNN9_9ACTN        Unreviewed;       406 AA.
AC   A0A094PNN9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGA12712.1};
GN   ORFNames=GM46_0650 {ECO:0000313|EMBL:KGA12712.1};
OS   actinobacterium acAcidi.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA12712.1, ECO:0000313|Proteomes:UP000029305};
RN   [1] {ECO:0000313|EMBL:KGA12712.1, ECO:0000313|Proteomes:UP000029305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT   "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT   sequencing.";
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:KGA12712.1}.
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DR   EMBL; JNSG01000006; KGA12712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094PNN9; -.
DR   Proteomes; UP000029305; 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; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          6..124
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          128..222
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..396
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   406 AA;  44526 MW;  5F946FFB1889D490 CRC64;
     MKPSYTPEAE AYRLKVQAFL KDNLPSDWKG IGTLEGKPLE EFVTQWRQVL AKGGYLAMGW
     PKQYGGGGLS ALEQVIAAEE FERAGVPTGG SNDVFSIQML GNTLLLFGTE EQKQHYLPRI
     IAGDDVWCQG YSEPNAGSDL SNVGLKAVLD GDEWILNGQK IWTSAGHLAD HIFTLARTDS
     DAPKHKGISF LLVDMRQQGI EVRPIKMISG ESEFNEVFYT DVRVPKENVV GGVNNGWAVA
     MGLLGFERGE AAATAPIRFQ AEIDRLMDLA REKGVASDPR IRQRLAKCYS VVQVMRYLGM
     RTLTQFLAGH HPGPDGAIFK LYWSEYHKVV TELGIDIMGM DALVPSGRKP SSAFQTDDAG
     APNDSMSWAT TFLNARAGTI YAGSSQVQRN IIGEMVLGLP KEPKPN
//
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