ID I4C456_DESTA Unreviewed; 380 AA.
AC I4C456;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AFM24347.1};
GN OrderedLocusNames=Desti_1636 {ECO:0000313|EMBL:AFM24347.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM24347.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-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}.
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DR EMBL; CP003360; AFM24347.1; -; Genomic_DNA.
DR RefSeq; WP_014809495.1; NC_018025.1.
DR AlphaFoldDB; I4C456; -.
DR STRING; 706587.Desti_1636; -.
DR KEGG; dti:Desti_1636; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_7; -.
DR OrthoDB; 9765339at2; -.
DR Proteomes; UP000006055; Chromosome.
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; 3.
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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000006055}.
FT DOMAIN 7..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..378
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 380 AA; 42688 MW; 2BFDC502B71D1AED CRC64;
MEIIKYTEEH NIFRQSLRKF LEKEVVPYVD QWEEAGIVPK SVWKKMGDQG FLCMNVPEEY
GGFGADFLYS VILSEELVRT GHTGLAAPLH SDVVVPYILS FGSEELKRQY LPPCVSGDAV
SAIAMTEPNT GSDLASIRTT AVEDGDHVIV NGQKTFISNG INCDIVVLAV RDPKETNPYA
AIDLYVVEAS TPGFEKGRNL KKIGWHSQDT AELFFNDCRV PKKNRLGEKG SGFLMLMNKL
QQERLMVCIS AVPAAEHMLE MTIKYCQERQ AFGKPISKFQ NTQFKIVEMA ADTKMARTFV
DKLIVDHMEG KNIVVEVSMA KYWTTEMATR VADTCLQLHG GYGYCEEYAI ARAWRDIRVM
QIFAGTNEIM KTIAAKFMGL
//
