ID V2IM73_9BURK Unreviewed; 383 AA.
AC V2IM73;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ESJ15945.1};
DE Flags: Fragment;
GN ORFNames=B551_0212670 {ECO:0000313|EMBL:ESJ15945.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ15945.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESJ15945.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:ESJ15945.1}.
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DR EMBL; AMPR02000188; ESJ15945.1; -; Genomic_DNA.
DR RefSeq; WP_023264184.1; NZ_AMPR02000188.1.
DR AlphaFoldDB; V2IM73; -.
DR OrthoDB; 2450120at2; -.
DR Proteomes; UP000053474; 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; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
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:SF20; ACYL-COA DEHYDROGENASE FADE28; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT DOMAIN 21..111
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 237..359
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT NON_TER 383
FT /evidence="ECO:0000313|EMBL:ESJ15945.1"
SQ SEQUENCE 383 AA; 41202 MW; 6E41554649C04F7C CRC64;
MNQREQSEQS ERELALELEL EQMLADSAQR LFDNEVTTAQ LEAAERGEWQ SALWQTVEDS
GLTRLFAGED DGGAAAGWQQ GLPALLAASR TLAPIPFIDT AVCGWVLAQL GIAMPDGPMA
LAAHVGDAEA ERPVARSSAE GWRLDGTVDV PWGRHVRHVV VRAVERQPFG RAVWLLAPTA
ACRVETSANL AGEPRDRLRF DDTLSAAAVV VEKPADEAML GPVAGSSQPS QPSPLGALMR
AIQIAGVLER VLNQTVQYAT ERIQFGRPIA KFQAIQQQLA MLANEVVAAR MAVASACAAM
RAPGWDSQAM VAKVICGNAA GRAAAIAHQV HGAIGFTHEH SLHWSTRRLW SWRAEYGSEA
HWAREIGAQA IRAGGAALWP RVT
//
