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Database: UniProt
Entry: E1WUE6_BACF6
LinkDB: E1WUE6_BACF6
Original site: E1WUE6_BACF6 
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
//
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