ID D0TXH1_9BACE Unreviewed; 568 AA.
AC D0TXH1;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acyl-CoA dehydrogenase, C-terminal domain protein {ECO:0000313|EMBL:EEZ01863.1};
GN ORFNames=HMPREF0102_04271 {ECO:0000313|EMBL:EEZ01863.1};
OS Bacteroides sp. 2_1_22.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ01863.1, ECO:0000313|Proteomes:UP000005775};
RN [1] {ECO:0000313|EMBL:EEZ01863.1, ECO:0000313|Proteomes:UP000005775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ01863.1,
RC ECO:0000313|Proteomes:UP000005775};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA McDonald J., Allen-Vercoe E., Strauss J., Ambrose C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 2_1_22.";
RL Submitted (JUL-2009) 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; GG705180; EEZ01863.1; -; Genomic_DNA.
DR RefSeq; WP_004314242.1; NZ_GG705180.1.
DR AlphaFoldDB; D0TXH1; -.
DR HOGENOM; CLU_018204_12_2_10; -.
DR Proteomes; UP000005775; 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; 63813 MW; 39932E7589BB15F0 CRC64;
MANYYTDIPE LKFHLNNPMM KRICELKERN YRDKDEFDYA PLDFEDAVDS YDKVLEITGE
ITGEIIAPNA EGVDEEGPHC ANGRVEYASG TKQNLDAMVK AGLNGMTMPR KFGGLNFPIT
PYTMCAEIVA AADAGFGNIW SLQDCIETLY EFGNSDQHSR FIPRICQGET MSMDLTEPDA
GSDLQSVMLK ATYSEKDGCW LLNGVKRFIT NGDADIHLVL ARSEEGTRDG RGLSMFIYDK
RQGGVNVRRI ENKLGIHGSP TCELVYKNAK AELCGDRKLG LIKYVMALMN GARLGIAAQS
VGLSQAAYNE GLAYAKDRKQ FGKAIIEFPA VYDMLAIMKG KLDAGRALLY QTSRYVDIYK
ALDDIARERK LTPEERQEQK KYAKLADSFT PLAKGMNSEY ANQNAYDCIQ IHGGSGFMME
YACQRIYRDA RITSIYEGTT QLQTVAAIRY VTNGSYIATI REFETIPCSP EMEPLMSRLK
KMADKFEAST NAVKEVQDQE LLDFTARKLV EMAADIIMCH LLIQDASKSS ELFSKSAHVY
LNYAEAEVEK HSNFIENFDK EDLAFYKK
//
