ID A0A0S8CDL6_9CHLR Unreviewed; 386 AA.
AC A0A0S8CDL6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KPK21955.1};
GN ORFNames=AMJ76_01305 {ECO:0000313|EMBL:KPK21955.1};
OS Dehalococcoidia bacterium SM23_28_1.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703395 {ECO:0000313|EMBL:KPK21955.1, ECO:0000313|Proteomes:UP000054497};
RN [1] {ECO:0000313|EMBL:KPK21955.1, ECO:0000313|Proteomes:UP000054497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_28_1 {ECO:0000313|EMBL:KPK21955.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK21955.1}.
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DR EMBL; LJTZ01000019; KPK21955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CDL6; -.
DR PATRIC; fig|1703395.3.peg.231; -.
DR Proteomes; UP000054497; 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; 1.10.540.10; 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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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 PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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 6..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 120..215
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 227..378
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 42184 MW; ADD7F78F38ADE48F CRC64;
MDYELTETHR LIRDTARRIA RERVQPRAAE IDEQGQYPED LFAVFRQAGL LGLTIPVEYG
GAGSFLALAL AVEETAKYCC SCGLILLLSA LSTQSIVVGG SEEQKQAWLP RSAAGDIRGA
YCLTEPNAGS DAAAIESRAR RDGDEYVIDG EKMFISGGSV AHFVITFAKT DPAAGTRGFS
AFIVPTDNPG FSVARLDRKM GVTGVPTANL VFQDCRVPAA NLIGEEGRGF RIAMLTMGTV
RPIVAARGLG LAQGALAYAL DFARERRTFG RPILEHQAIQ FMLADMATQI EAARHLVYHA
CWLIDQGKYD RQYAPYFSFA KVFATEMAVK VSSDALQILG AQGYMKDHPL ERHYRDARQL
MIVEGTSQVQ RMIITRGLAD GDIVYG
//
