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Database: UniProt
Entry: R6M8J1_9BACE
LinkDB: R6M8J1_9BACE
Original site: R6M8J1_9BACE 
ID   R6M8J1_9BACE            Unreviewed;       568 AA.
AC   R6M8J1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Acyl-CoA dehydrogenase C-terminal domain protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN659_01784 {ECO:0000313|EMBL:CDB95918.1};
OS   Bacteroides sp. CAG:443.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262739 {ECO:0000313|EMBL:CDB95918.1, ECO:0000313|Proteomes:UP000018098};
RN   [1] {ECO:0000313|EMBL:CDB95918.1, ECO:0000313|Proteomes:UP000018098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:443 {ECO:0000313|Proteomes:UP000018098};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB95918.1}.
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DR   EMBL; CBEN010000007; CDB95918.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6M8J1; -.
DR   Proteomes; UP000018098; 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   Coiled coil {ECO:0000256|SAM:Coils};
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          91..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"
FT   COILED          472..499
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   568 AA;  64028 MW;  79185FF34238F049 CRC64;
     MANFYTEHPE LKFHLNNPMM ERICQLKERD YRDKDEYDYA PQDYTDAIDS YDKVLEITGE
     ITGEVIAANA EGVDQEGPHH ANGRVEYASG TKANLDAMVK AGLNGMTMPR RFGGLNFPIT
     PYTMCAEIVA QADAGFGNIW SLQDCIETLY EFGNEDQHSR FIPRICAGET MSMDLTEPDA
     GSDLQSVMLK ATYDEANNCW RLNGVKRFIT NGDANLHLVL ARSEEGTHDG RGLSMFIYDK
     NDGGVDVRRI ENKLGIHGSP TCELVYKNAK AELCGDRKLG LIKYVMALMN GARLGIAAQS
     VGLSQAAYDE ALAYAKDRKQ FGKAIIEFPA VYDMLATIKA KLDAGRALLY QTSRYVDIYK
     ALDDIARERK LTPEERQEQK RYAKLADSFT PLAKGMNSEY ANQNAYDCIQ VHGGSGFMME
     YACQRIYRDA RITSIYEGTT QLQTVAAIRY VTNGAYAATL HEYETIPCAP EYENYMNRIK
     EMTRKLEACT NAVKEAQNQE LLDFVARRLY EMAAVCVMSH LLLQDATKAP DLFGKSLNVY
     VNYAESEVEK HFNFIRKFNA EELANYRK
//
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