ID E1WUE6_BACF6 Unreviewed; 567 AA.
AC E1WUE6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:CBW23707.1};
GN OrderedLocusNames=BF638R_3231 {ECO:0000313|EMBL:CBW23707.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23707.1, ECO:0000313|Proteomes:UP000008560};
RN [1] {ECO:0000313|EMBL:CBW23707.1, ECO:0000313|Proteomes:UP000008560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R {ECO:0000313|EMBL:CBW23707.1,
RC ECO:0000313|Proteomes:UP000008560};
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
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; FQ312004; CBW23707.1; -; Genomic_DNA.
DR RefSeq; WP_005789707.1; NC_016776.1.
DR AlphaFoldDB; E1WUE6; -.
DR KEGG; bfg:BF638R_3231; -.
DR PATRIC; fig|862962.3.peg.3335; -.
DR HOGENOM; CLU_018204_12_2_10; -.
DR OMA; FPAVYDM; -.
DR Proteomes; UP000008560; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 1.
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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
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; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF158494; PG0775 C-terminal domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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 95..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 173..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 452..562
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 567 AA; 63678 MW; 057FE5796E0E9FB8 CRC64;
MANFYLDTPE LKHHLNHPLM KRIVELKERN YADKDKFDYA PVDFEDAMDS YDKVLEIVGE
ICGDIIAPNA EGVDHEGPVC ADNRVTYASG TTRNLDACRK AGLMGMAMPR RFGGLNFPIT
PYIMAADIVS RSDAGFENLW GLQDCAETIY EFANEEQKQR YITRVCQGET MSMDLTEPDA
GSDLQSVMLK ATYSEKDQCW YLNGVKRFIT NGDADIHLVL ARSEEGTHDG RGLSMFIYDK
RNGGVNVRRI ENKMGIKGSP TCELVYKNAK AELCGDRKLG LIKYVMALMN GARLGIAAQS
VGLSQAAYNE ALAYAKDRKQ FGKAIIEFPA VAEILSLMKA KLDASRSLLY ETARFVDVYK
ALDDIAKERK LTPEERAEQK TFAKLADAFT PLGKGMGSEF ANQNAYDCIQ IHGGSGFMKD
YACERIYRDS RITSIYEGTT QLQVVAAIRY VTTGAYLARI QEYENMPVAP ELEGLQNRLK
SMASKYAACV TQITEAKDQE LLDFCARRLV EMAAHIIMGH LMVQDASKSD LFSESAQVYV
RYAEAEVEKH INFIRKFDKD DLAYYRK
//