ID A0A085VFB2_PSESX Unreviewed; 600 AA.
AC A0A085VFB2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KFE54125.1};
GN ORFNames=IV01_17455 {ECO:0000313|EMBL:KFE54125.1};
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317 {ECO:0000313|EMBL:KFE54125.1, ECO:0000313|Proteomes:UP000028631};
RN [1] {ECO:0000313|EMBL:KFE54125.1, ECO:0000313|Proteomes:UP000028631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAW0119 {ECO:0000313|EMBL:KFE54125.1,
RC ECO:0000313|Proteomes:UP000028631};
RA Baltrus D.A., Berge O., Morris C.;
RT "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL Submitted (JUL-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:KFE54125.1}.
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DR EMBL; JPQU01000048; KFE54125.1; -; Genomic_DNA.
DR RefSeq; WP_032629995.1; NZ_JPQU01000048.1.
DR AlphaFoldDB; A0A085VFB2; -.
DR PATRIC; fig|317.175.peg.3637; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000028631; 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:SF3; ACYL-COA DEHYDROGENASE-RELATED; 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|RuleBase:RU362125}.
FT DOMAIN 9..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 43..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 285..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 471..595
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 600 AA; 66157 MW; 1CE87DD738E23A90 CRC64;
MSELLLSSRN LAFELYEVLD AEALTRRERF AEHNRETFDA AIGTARAIAE KYFAPHNRKA
DENEPRYENG EAILIPEVKP AVDAFLEAGF LNATRGFEDG GMQLPTLLSQ ACFAHFQAAN
AGSTAYPFLT MGAANLIESF GSDAQKQQFL KPMIEGRFFG TMALTEPHAG SSLSDIRTRA
EPAEDGTYRL RGNKIFISGG DHQLSENIVH MVLAKLPDAP AGVKGISLFI VPKLLVKEDG
SLGSRNDVIL AGLFHKMGWR GTTSTALNFG DNGQCVAYLV GKPHQGLSYM FQMMNEARIG
VGMGAVMLGY AGYLYSLDYA RERPQGRLPD SKSPDSAPVP IIEHADVRRM LLTQKAYVEG
AFDLGLYAAR LFDDTTTGET EAVRQQAQKL LDLLTPIVKA WPSEFCLKAN ELAIQVLGGH
GYTREYPVEQ YYRDNRLNPI HEGTNGIQSL DLLGRKLAQD GGAGLKQLLR LIAETSQRAQ
AHETLTELRQ PLEHLVAHLQ TVTLALLGDL AQGKVNAALA NSALYLKAFG HTVIGWRWLE
QAIHAQQGLA NGNVADKDFY QGKLQAARYF LTWEVPSCHH ELAILEARDD TCLAMRDCWF
//
