ID U2BFB5_9PSED Unreviewed; 597 AA.
AC U2BFB5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ERI53896.1};
GN ORFNames=N878_13685 {ECO:0000313|EMBL:ERI53896.1};
OS Pseudomonas sp. EGD-AK9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI53896.1, ECO:0000313|Proteomes:UP000016488};
RN [1] {ECO:0000313|EMBL:ERI53896.1, ECO:0000313|Proteomes:UP000016488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA Purohit H.J.;
RT "Indian agricultural soil isolates capable of pesticide degradation.";
RL Submitted (AUG-2013) 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:ERI53896.1}.
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DR EMBL; AVOF01000060; ERI53896.1; -; Genomic_DNA.
DR RefSeq; WP_021442263.1; NZ_AVOF01000060.1.
DR AlphaFoldDB; U2BFB5; -.
DR PATRIC; fig|1386078.3.peg.627; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000016488; 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..29
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 41..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 466..591
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 597 AA; 64202 MW; E3229DB125DDDC92 CRC64;
MPEYKAPLRD MRFLIDDVFA FPAHYAALDA SEASPDMLGA ILEEGAKFCE QVLAPLNRSG
DEEGCRFDAG VVSTPKGFKE AFAQYAEGGW MGLAADPAYG GQGLPQSLGL IVSEMVASAN
QSWAMYPGLT HGAMSAIHAH GSEAQKQTYL SRMSEGRWTG TMCLTEAHCG TDLGLIKTRA
VPQADGSYRI SGSKIFISAG EHDMSENIVH LVLAKLPDAP AGTRGISLFI VPKFLPDATG
EAGARNAVSC GAIEHKMGIK ASSTCVINFD GASGYLIGEA NKGLACMFTM MNHARLGTGM
QGLCLGEASF QGALKYANER LQMRALSGPK APDKAADPII VHPDVRRMLL TMKAFNEGNR
ALAYFTAQLL DVAHQAESAE AREEAENLLA FLTPICKAFM TETGLEATNL GMQVFGGHGY
IREWGMEQLV RDCRIAPIYE GTNGIQALDL LGRKVLGSQG KLLRGFTKIV HKFCEAQAGH
PQLGAQVAQL AALNKQWGEL TQQVGMAAMK NPDEVGAASV DYLMYSGYLT LAYFWLRMAV
VAQEKLAAGD DDGFHQAKLA TCAFYFQRLL PRTEAHRLAL AAGSACMMEL PAEHFAF
//
