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Database: UniProt
Entry: A0A3N1LIG8_9PROT
LinkDB: A0A3N1LIG8_9PROT
Original site: A0A3N1LIG8_9PROT 
ID   A0A3N1LIG8_9PROT        Unreviewed;       413 AA.
AC   A0A3N1LIG8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EDC65_3193 {ECO:0000313|EMBL:ROP91327.1};
OS   Stella humosa.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Stellaceae; Stella.
OX   NCBI_TaxID=94 {ECO:0000313|EMBL:ROP91327.1, ECO:0000313|Proteomes:UP000278222};
RN   [1] {ECO:0000313|EMBL:ROP91327.1, ECO:0000313|Proteomes:UP000278222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5900 {ECO:0000313|EMBL:ROP91327.1,
RC   ECO:0000313|Proteomes:UP000278222};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) 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:ROP91327.1}.
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DR   EMBL; RJKX01000014; ROP91327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1LIG8; -.
DR   OrthoDB; 5510711at2; -.
DR   Proteomes; UP000278222; 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   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; 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; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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   PIRSF; PIRSF016578; HsaA; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278222}.
FT   DOMAIN          6..109
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..384
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   413 AA;  44036 MW;  39DCA02AF6CBB3FA CRC64;
     MPLGLTTEER ALQARAAEFA ATVVRPQAAE TDRSEQYPWD VVKALAAAGF TGMTVPRAYG
     GQGASFLDAV LVIEEMAKAC TVTARIVVEA NMGAISTVMA YGSERQKRMA ADLVLAGDKP
     AICITEPDAG SDATAMTTRA DRVGDRFVLN GRKHWITGAG VSKLHLIFAR AFDEKGRNLG
     IGGFLAVRGE APGLKMVRRE QTMGLRGMPE GELAFEDLEV ADDMVVMPPS GWARGFGDLI
     NAYNSQRVGA GTVAMGVAAG AFEHAVAFAK EREQFGRPIG EFQGLQWMLA DMQTQLTASR
     LMLYAAARSR GPNGSAFPDP ALAAQAKIFA SEAAVRIAND ALQLHGARGY SRELPLERMV
     RDCRMFTIGG GTAQVLRTLV ASKILGWKLP QTRDGYVRNN PPGAAGSGRD AAE
//
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