GenomeNet

Database: UniProt
Entry: U6RLE5_9BACE
LinkDB: U6RLE5_9BACE
Original site: U6RLE5_9BACE 
ID   U6RLE5_9BACE            Unreviewed;       568 AA.
AC   U6RLE5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1214_03019 {ECO:0000313|EMBL:EOA56576.1};
OS   Bacteroides sp. HPS0048.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1078089 {ECO:0000313|EMBL:EOA56576.1, ECO:0000313|Proteomes:UP000017815};
RN   [1] {ECO:0000313|EMBL:EOA56576.1, ECO:0000313|Proteomes:UP000017815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPS0048 {ECO:0000313|EMBL:EOA56576.1,
RC   ECO:0000313|Proteomes:UP000017815};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. HPS0048.";
RL   Submitted (APR-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:EOA56576.1}.
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DR   EMBL; AGEU01000044; EOA56576.1; -; Genomic_DNA.
DR   RefSeq; WP_002560944.1; NZ_KB905489.1.
DR   AlphaFoldDB; U6RLE5; -.
DR   PATRIC; fig|1078089.3.peg.2963; -.
DR   HOGENOM; CLU_018204_12_2_10; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000017815; Unassembled WGS sequence.
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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          59..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..563
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12186"
SQ   SEQUENCE   568 AA;  63723 MW;  25777656308389FF CRC64;
     MANFYLDTPE LKHHLSHPLM KRIVELKERN YADKDNFDYA PIDFEDAMDS YDKVLEIVGE
     ICGDIIAPNA ENVDHEGPVC ANNRVTYANG TAANLEACRK AGLMGMAMPR RFGGLNFPIT
     PYIMAADIVS RSDAGFENLW GLQDCAETIY EFANEDQKKR YITRVCQGET MSMDLTEPDA
     GSDLQAVMLK ATYSEKDQCW YLNGVKRFIT NGDSDIHLVL ARSEEGTHDG RGLSMFIYDK
     RNGGVNVRRI ENKMGIKGSP TCELVYKNAK AELCGDRKLG LIKYVMALMN GARLGIAAQS
     VGISQAAYNE ALAYAQDRKQ FGKAIIEFPA VAEILSLMKA KLDASRTLLY ETARFVDVYK
     ALDDIAKERK LTPEERAEQK TFAKLADAFT PLGKGMGSEF ANQNAYDCIQ IHGGSGFMKD
     YACERIYRDA RITSIYEGTT QLQVVAAIRY VTTGAYLNRI KEYENMPVAP EMEGLHNRLK
     TMASKYAACV AQITEAKDQE LLDFCARRLV EMAAHIIMGH LLVQDASKNA ELFGTSAQVY
     VRYAESEVEK HINFIRKFDK DDLAYYRK
//
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