ID A0A1I7JHT5_9BURK Unreviewed; 419 AA.
AC A0A1I7JHT5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SFU84753.1};
GN ORFNames=SAMN05216552_1011158 {ECO:0000313|EMBL:SFU84753.1};
OS Pseudoduganella namucuonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=1035707 {ECO:0000313|EMBL:SFU84753.1, ECO:0000313|Proteomes:UP000199391};
RN [1] {ECO:0000313|Proteomes:UP000199391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11014 {ECO:0000313|Proteomes:UP000199391};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; FPBO01000011; SFU84753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7JHT5; -.
DR STRING; 1035707.SAMN05216552_1011158; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000199391; 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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000199391}.
FT DOMAIN 12..134
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 138..239
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..399
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 419 AA; 47009 MW; 50566774572BBECB CRC64;
MDFEYSDRCK ELQGKLLAFM DQHIYPNEQV FHDEIERNGR EKNNRWLPTE IIEKLKPLAR
EQGLWNLFLP KSTRAPEGLS NLDYAPLCEI MGRVHWAPEV FNCAAPDTGN METLERYGSE
EHKRLWLEPL LRGEIRSAFA MTEPAVASSD ATNIEMKIER DGDDYVINGR KWWISGAGDP
RCKIYITMGK TDFGAARHQQ QSMILVPADT PGITVLRPLP VFGYDDAPHG HCEIVYDNVR
VPASNILLGE GRGFEIAQGR LGPGRIHHCM RAIGVAERAL ELMCKRLNGR TAFGKRISEQ
GVWRERIAEA RIQIDTARLL TLKAAYMMDK VGNKGAQAEI AMIKVLAPNV TQQVLDWAIQ
AHGAGGVSGD FPLAYQWAGN RTLRLADGPD EVHRNAIAKL ELAKHIDLKE DLGLPVTRG
//
