ID A0A135VSJ1_9ARCH Unreviewed; 400 AA.
AC A0A135VSJ1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AM325_16160 {ECO:0000313|EMBL:KXH75636.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-45.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706444 {ECO:0000313|EMBL:KXH75636.1, ECO:0000313|Proteomes:UP000070149};
RN [1] {ECO:0000313|EMBL:KXH75636.1, ECO:0000313|Proteomes:UP000070149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-45 {ECO:0000313|EMBL:KXH75636.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
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:KXH75636.1}.
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DR EMBL; LRSL01000006; KXH75636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VSJ1; -.
DR STRING; 1706444.AM325_16160; -.
DR Proteomes; UP000070149; 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; ISOVALERYL-COA DEHYDROGENASE, 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM 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|RuleBase:RU362125}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..216
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 400 AA; 43660 MW; 961D86E02BCA4560 CRC64;
MDFALTEKEQ KLWERAKEFT YEHITPRAHE LERKNEFPKD VVQKAYEAGL MNLHIPTEAG
GPGLSLLAET LVSEATGYGC AGLATTIMCN NLAFAPLVIG ATTEQLQTYI EPLITGKEAK
FGAFSLTERK AGSDAAAVAT RATRDGDEYV INGMKCWITN APVASLFTVF ASTQPELKHK
GLSVFMVPKS KNVKIGHIEN KVGQLNSIQS EVFFEDARVP RDCLVGKEGD GFKIAMMTLD
KTRAGIAAIA TGVAQRAVDE AAKFANIRHQ FGQPIGAFQG ISFTLADMGA KTAAARWQTR
YAAWLADQDL PNSKDSAFAK FFASDTAMQN AIECVQIMGG YGYINEYPAE KLLRDAKLLQ
IYEGTNQVQR LVAGNAILKE SVNLDTGFRF KYDGQDAPSL
//