ID F6F1Q2_SPHCR Unreviewed; 576 AA.
AC F6F1Q2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AEG51468.1};
GN ORFNames=Sphch_3886 {ECO:0000313|EMBL:AEG51468.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG51468.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG51468.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG51468.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 2 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) 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; CP002799; AEG51468.1; -; Genomic_DNA.
DR RefSeq; WP_013849692.1; NC_015594.1.
DR AlphaFoldDB; F6F1Q2; -.
DR STRING; 690566.Sphch_3886; -.
DR KEGG; sch:Sphch_3886; -.
DR HOGENOM; CLU_018204_12_2_5; -.
DR Proteomes; UP000007150; Chromosome 2.
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; 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 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 39..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 160..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..445
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 462..571
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 576 AA; 60941 MW; B507496B88E22145 CRC64;
MFSYVPPIDD YRFLLTQVLG FDRAMAETGK DVDADLAAAV LEEAGRMCAE RLHPINRHGD
EEGSRLIDGE VHTPEGFADA WRDFVAAGWP SLAAAPEYGG QGLPFILQLW LDEMLAAANM
SFGLFPGLTR GACEAIAAHA DDSLKATYLS RMVSGEWTGA MALTESGAGT DLALLKAKAV
PDADGGYAVT GQKIFISSGD HDFGGNIIHL VLARLPDAPA GVKGISLFLV PKYLPDADGN
FTVRNAMSVG ALEKKMGIHA QPTCVMNYDG ATGWLVGEPH RGLAAMFTMM NAERLMVGIQ
GLGIAGAAYQ QAAGYAKERL QGRSADGTRE PVAIIEHADV RRMLLNIRAF VEGARALGGW
TALQLDRAHH HEDAAERAKA DGLVALLTPV VKAAFTDYGF ESAVQAQQVF GGHGYIREWG
MEQYVRDARI AQIYEGTNGV QAMDLVGRKL PMAGGAVVEG FFALVADDLG AAGASGIAVS
TREALALLRE VTASLRGAGV EAAGAAAADY LRLFALVSMG WMWTRMAAAE GDTPLHDAKR
AVADFFAQRM LPQVRGLAGS IAAGEATIMA LAADAF
//
