ID A0A159ZBR4_9RHOB Unreviewed; 388 AA.
AC A0A159ZBR4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:AMY72324.1};
GN ORFNames=AKL17_3p0168 {ECO:0000313|EMBL:AMY72324.1};
OS Frigidibacter mobilis.
OG Plasmid cai42_Plasmidc {ECO:0000313|Proteomes:UP000076128}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY72324.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY72324.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RC PLASMID=Plasmid cai42_Plasmidc {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) 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; CP012664; AMY72324.1; -; Genomic_DNA.
DR RefSeq; WP_066819364.1; NZ_CP012664.1.
DR AlphaFoldDB; A0A159ZBR4; -.
DR KEGG; daa:AKL17_3p0168; -.
DR PATRIC; fig|1335048.3.peg.5293; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000076128; Plasmid cai42_Plasmidc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; 2.
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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Plasmid {ECO:0000313|EMBL:AMY72324.1}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..366
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 388 AA; 42772 MW; 9854C7CB25B56A7D CRC64;
MDFELTQEQE AIRDAVAAVC AKFDDSYWLT RDREGGFPHD FYDALARDGW LGVCTPEAYG
GAGLGITEAA LVMRTIAESG AGMSGASAVH INIFGLNPVS VFGTEEQKAR MMRPMAEGRE
KACFAVTEPS TGLNTTQLKL RAVKTGDRYV VNGQKVWIST AQEADRILLL ARTTPIDQID
KPTRGLSLFY TRFDRSRIRV QEIEKMGRKC VDSNELFFDD FEIPEADLIG EEGRGFEYIL
HGMNPERVLI AAEAVGLGML AIDRAAEYAK ERIVFNRPIG QNQGIQHPLA KCWAELEAAW
MMVLAAASRY DRGLPCGAAA NAAKYLAGEA GFTACETAVM AHGGFGYAKE YHVERYLREA
FIPRIAPISP QLCLSYLAER VLGLPKSY
//
