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Database: UniProt
Entry: A0A135VSJ1_9ARCH
LinkDB: A0A135VSJ1_9ARCH
Original site: A0A135VSJ1_9ARCH 
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
//
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