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Database: UniProt
Entry: D7KA99_9BACE
LinkDB: D7KA99_9BACE
Original site: D7KA99_9BACE 
ID   D7KA99_9BACE            Unreviewed;       568 AA.
AC   D7KA99;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:EFI36498.1};
GN   ORFNames=HMPREF9010_04549 {ECO:0000313|EMBL:EFI36498.1};
OS   Bacteroides sp. 3_1_23.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=457390 {ECO:0000313|EMBL:EFI36498.1, ECO:0000313|Proteomes:UP000003808};
RN   [1] {ECO:0000313|EMBL:EFI36498.1, ECO:0000313|Proteomes:UP000003808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_23 {ECO:0000313|EMBL:EFI36498.1,
RC   ECO:0000313|Proteomes:UP000003808};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA   Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 3_1_23.";
RL   Submitted (MAR-2010) 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; GG774960; EFI36498.1; -; Genomic_DNA.
DR   RefSeq; WP_004301030.1; NZ_GG774960.1.
DR   AlphaFoldDB; D7KA99; -.
DR   SMR; D7KA99; -.
DR   GeneID; 29455645; -.
DR   HOGENOM; CLU_018204_12_2_10; -.
DR   Proteomes; UP000003808; 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          92..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;  63710 MW;  897D379D1DA65081 CRC64;
     MANYYTDIPE LKFHLNNPMM KRICELKERN YRDKDEFDYA PLDFEDAVDS YDKVLEITGE
     ITGEIIAANA EGVDEEGPHC ANGRVEYASG TKQNLDAMVK AGLNGMTMPR RFGGLNFPIT
     PYTMCAEIVA AADAGFGNIW SLQDCIETLY EFGNADQHSR FIPRVCQGET MSMDLTEPDA
     GSDLQAVMLK ATYSEKDGCW LLNGVKRFIT NGDANLHLVL ARSEEGTRDG RGLSMFIYDK
     NEGGVNVRRI ENKLGIHGSP TCELVYKNAK AELCGDRKLG LIKYVMALMN GARLGIAAQS
     VGLSQAAYNE GLAYAKDRKQ FGKAIIEFPA VYDMLAIMKG KLDAGRALLY QTARYVDIYK
     ALDDISRERK LTPEERQEQK KYAKLADSFT PLAKGMNSEY ANQNAYDCIQ IHGGSGFMME
     YACQRIYRDA RITSIYEGTT QLQTVAAIRY VTNGSYIATI REFEAIPCSP EMEPLMSRLK
     KMADKFEAST NAVKEVQDQE LLDFTARKLV EMAADIIMCH LLIQDASKSS ELFSKSAHVY
     LNYAEAEVEK HTNFIENFDK EDLAFYKK
//
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