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Database: UniProt
Entry: A0A1I2IEA5_9GAMM
LinkDB: A0A1I2IEA5_9GAMM
Original site: A0A1I2IEA5_9GAMM 
ID   A0A1I2IEA5_9GAMM        Unreviewed;       591 AA.
AC   A0A1I2IEA5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN02799615_03403 {ECO:0000313|EMBL:SFF39973.1};
OS   Dyella marensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=500610 {ECO:0000313|EMBL:SFF39973.1, ECO:0000313|Proteomes:UP000199477};
RN   [1] {ECO:0000313|EMBL:SFF39973.1, ECO:0000313|Proteomes:UP000199477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNC178MFTsu3.1 {ECO:0000313|EMBL:SFF39973.1,
RC   ECO:0000313|Proteomes:UP000199477};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FONH01000016; SFF39973.1; -; Genomic_DNA.
DR   RefSeq; WP_026635679.1; NZ_FONH01000016.1.
DR   AlphaFoldDB; A0A1I2IEA5; -.
DR   STRING; 500610.SAMN02799615_03403; -.
DR   Proteomes; UP000199477; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_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          4..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          82..159
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          165..274
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          285..452
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          469..587
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   591 AA;  63524 MW;  E52079B03A83C49D CRC64;
     MTIYKAPLDD LRFALYDVLH AEATLTQLQG GEGHTRDLLD AVLEEAGRLS EALLAPFNAS
     GDEEGCKYDK ATQTVTTPKG FKEAFKAFAE GGWTGLTQAE HFGGQGLPNT VGTATTEIFQ
     AGNLSWSLYP LLSEGACHAM ELHGTKEQQD TYLKPIVEGR WTGTMCLTEP QAGSDLGLLK
     TRAEPGDNGS YKITGTKIFI SAGEHDLAEN IIHLVLARLP DAPAGSRGIS MFIVPKFKLN
     ADGSPGTRNT VVASNIEHKM GLRGSATCVM NFDAAEGYLI GQPHKGLAAM FTMMNAARLG
     VGVQGLALSE RALQNSSNYA RERLQGRALS GPQFPDKPAD NLLVQPDVRR MLLTQRAIVE
     GSRTLLLYTS LQTDVEARGV DEVTRKNAGE LVAFLIPIAK GLVTELAQES TKEALQVYGG
     HGYIVESGVE QFVRDARIIT LYEGTTGIQA ADLLGRKILQ LQGAGFKLFL QEIQAFCQKH
     AQDAAMASLI APLARNAKEW ADLTLAVAAR VQGNPEELGA AASDYLYYSG YATLAYMWAR
     SVAAANASSQ SEAFKQSKRD TAAFYFARML PRCLMHKAAI EAGVGTLPAV A
//
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