ID A0A0A1F7L0_9BURK Unreviewed; 596 AA.
AC A0A0A1F7L0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AIY39750.1};
DE EC=1.3.8.7 {ECO:0000313|EMBL:AIY39750.1};
GN ORFNames=LT85_0590 {ECO:0000313|EMBL:AIY39750.1};
OS Collimonas arenae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY39750.1, ECO:0000313|Proteomes:UP000030302};
RN [1] {ECO:0000313|EMBL:AIY39750.1, ECO:0000313|Proteomes:UP000030302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cal35 {ECO:0000313|EMBL:AIY39750.1,
RC ECO:0000313|Proteomes:UP000030302};
RA Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT "Structure and function of bacterial communities in ageing soils: insights
RT from the Mendocino ecological staircase.";
RL Soil Biol. Biochem. 69:265-274(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009962; AIY39750.1; -; Genomic_DNA.
DR RefSeq; WP_038485049.1; NZ_CP009962.1.
DR AlphaFoldDB; A0A0A1F7L0; -.
DR STRING; 279058.LT85_0590; -.
DR KEGG; care:LT85_0590; -.
DR HOGENOM; CLU_018204_12_2_4; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000030302; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AIY39750.1}.
FT DOMAIN 3..35
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 82..160
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 165..273
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 470..592
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 596 AA; 65107 MW; 4148A7B9A0FAE5E5 CRC64;
MGQYVAPLRD MQFVMHELLH VEDELKQLPK HAEIDADIIN QVLEEGGKFT SQVLFPLNHS
GDREGCHHDK ATHTVTAPKG FKEAYKQYVE AGWPSLSCDP DFGGQGLPLV INNSFYEMMN
SANQAWTMYP GLSHGAYECL HAHGTPEQQA LYLPKLVSGE WTGTMCLTEA HCGTDLGMLR
SKAEPQADGS YKITGSKIFI SAGEHDMSAN ILHLVLARLP GAPEGSKGIS LFLVPKFLPN
ADGSLGERNP ITCGAIEEKM GIHGNSTCQM NLDGATGWII GGPHKGLNAM FVFMNAARLG
VGMQGLGLTE VAYQNALVYA KDRIQMRSLS GIKAPDKPAD PIIVHPDVRR MLLTAKAYAE
GARAFCSYVA LQLDKELNHP DEEVRKNAAD EVALLTPVIK AFITDNAWVA TSECMQVYGG
HGFIAEWGME QYVRDARINM IYEGTNTIQS LDLLGRKVLM DNGAKLKKFG AKVQAFIEEN
GADESLSEFI TPLADLGDKV SKLTMEIGMK AFQNPDEAGA AAVPYLRVVG HLVYAYFFAQ
MAKIALAKQD SGDKFYVSKL ATARFYFARL LPETAMLIRQ ARSGSGSLMA LDADLF
//
