ID A0A1E4M9X5_9SPHN Unreviewed; 406 AA.
AC A0A1E4M9X5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ODU67524.1};
GN ORFNames=ABT11_19915 {ECO:0000313|EMBL:ODU67524.1};
OS Novosphingobium sp. SCN 66-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1660121 {ECO:0000313|EMBL:ODU67524.1, ECO:0000313|Proteomes:UP000094170};
RN [1] {ECO:0000313|EMBL:ODU67524.1, ECO:0000313|Proteomes:UP000094170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU67524.1}.
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DR EMBL; MEGD01000060; ODU67524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4M9X5; -.
DR Proteomes; UP000094170; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 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.
PE 4: Predicted;
FT DOMAIN 31..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 251..380
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 406 AA; 43390 MW; F3037ABDDB7268D1 CRC64;
MTVASDLSIV SKWPTIGSAQ EAIAKVRALL PEIEQADTGA DSNRRLDAGV VDRMRASGLF
GLVMPRNLGG SELGFADLVR VATEIGSVSG SAAWIFGVLA GHSWLINLFP EQAQREVMGD
PTTLIGTVFR LGGDVVEEGD GYRLTGGNGK FCSGIDYATW VIIGNAVKKA DGSMEPRFFV
VPKTDIEVID DWQTMGMRAT GSRSIRIDSA FIPAHRSCSL ADMLAGSTPG AKHHSGAVYR
MPFSNIAPFS IVGAPLGMAK GMVTRFAGEL GAKLDGASPL EVAEQSATLA RIAEVDAHID
AALALVISDA EMIDHAIEPD DISFLQSARI PRNWAWAVQQ ARHAANRIFE ASGGTAIYDD
QKIQQLFRDI NAAAQHFAFT WDRAMTAYGR AATGLKPGEF AIPKRN
//
