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Database: UniProt
Entry: A0A1H2EDH7_9PSED
LinkDB: A0A1H2EDH7_9PSED
Original site: A0A1H2EDH7_9PSED 
ID   A0A1H2EDH7_9PSED        Unreviewed;       588 AA.
AC   A0A1H2EDH7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05216580_0512 {ECO:0000313|EMBL:SDT93063.1};
OS   Pseudomonas guangdongensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245526 {ECO:0000313|EMBL:SDT93063.1, ECO:0000313|Proteomes:UP000243063};
RN   [1] {ECO:0000313|Proteomes:UP000243063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC 2012022 {ECO:0000313|Proteomes:UP000243063};
RA   Varghese N., Submissions S.;
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; LT629780; SDT93063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2EDH7; -.
DR   STRING; 1245526.SAMN05216580_0512; -.
DR   OrthoDB; 9764895at2; -.
DR   Proteomes; UP000243063; Chromosome i.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243063}.
FT   DOMAIN          3..32
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          41..159
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          163..272
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          284..455
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          468..583
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   588 AA;  63109 MW;  E04317C15A93BCE0 CRC64;
     MADYQAPLRD MRFVLEELLD VPAQWAALPR LAGSLDADIA RAVLEEAARL CAQRLAPLNR
     SGDEEGCQWR AEGVATPAGF AAAWRAWAEG GWVGLSGEAE HGGLGMPKAL AAQVEELLNA
     ANLSFALYPM LSAGAALTLA AHADATLRAL YLPRLYRGEW AGAMCLTEPQ AGTDLGLIRT
     RAEPDGDGSY RIFGGKIFIT GGEHDLTPNI VHLLLARLPD APPGSKGVSL FLVPKFLVEA
     DGSLGARNAM SCGALEHKMG IKASSTCVMH YDGARGWLVG APHQGLAAMF TMMNYERLGV
     GIQGLAAGER SWQNARAYAR ERLQGRAPGG AVAPGLSADP IVAQPDVRRM LLTMRALTEG
     GRAFSSYVAS QLDLARDAPQ PDLRAAAEAR VALLTPVAKA FLTDLGLEVC VLGQQVFGGH
     GYIREWGQEQ LVRDVRITQI YEGTNGIQAL DLAGRKLVAD GGALYRAFAA EMRADLDTAG
     EFAAPLAAAL DNLDALSDWL IERGRRDPRE VGAASVEYLQ VFGYTVYAWL WARMARLALA
     REAQEVFYAE KLATARFYFA RLLPRIHALS AALRSGSAVL YEVPESLL
//
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