ID A0A0B1YDI1_9RALS Unreviewed; 583 AA.
AC A0A0B1YDI1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Isovaleryl-CoA dehydrogenase {ECO:0000313|EMBL:KHK56575.1};
GN ORFNames=PI87_09215 {ECO:0000313|EMBL:KHK56575.1};
OS Ralstonia sp. A12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1217052 {ECO:0000313|EMBL:KHK56575.1, ECO:0000313|Proteomes:UP000030970};
RN [1] {ECO:0000313|EMBL:KHK56575.1, ECO:0000313|Proteomes:UP000030970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A12 {ECO:0000313|EMBL:KHK56575.1,
RC ECO:0000313|Proteomes:UP000030970};
RA Chen J.W., Yin W.F., Chan K.G.;
RT "Draft Genome of Ralstonia A12.";
RL Submitted (NOV-2014) 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}.
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:KHK56575.1}.
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DR EMBL; JSZO01000006; KHK56575.1; -; Genomic_DNA.
DR RefSeq; WP_039597420.1; NZ_JSZO01000006.1.
DR AlphaFoldDB; A0A0B1YDI1; -.
DR STRING; 1217052.PI87_09215; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000030970; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 1.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 16..172
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 178..281
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 292..448
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 583 AA; 64227 MW; 8CFE289A5DDE9195 CRC64;
MNDIAREPLI GHQNIPDSRG INFFHVDPDL ARLLRLYLGD AQYRALEPQL KSLGLRASDE
LDAWAINADH NPPQLRHRTR RGEALQSIDK HPDYVALERV AYAELGLASM SHVGNAPPPL
VKYALTYLFV QAEFGLCCPV SMTDSLTRTL RKFGDPGLVA RYLPMLASRD FDVLYQGAMF
MTEQAAGSDV ARIATRAARE TAPDGTQTWR LYGDKWFCSN ADADLAMVLA RPDGAPPGIN
GLALFLLPKT LRDGSRNHYR IVRLKDKLGT RSMASGEIVL EGATAYLIGE IGRGFHQMAD
MINMSRLSNG VRAAGLMRRA TTEALHIARN REAFGRKLID MPLMQRQLLK MLLPTEQARS
MFMQIAQLLP LADAGDAQAA KCVRILTPLI KFRACRDARR VTGDAMEVRG GTGYIEEWSD
ARLVRDSHLG SIWEGTSNIV ALDIARAVKR EGALEPLRAY LSGLLDGVTL PTQSDALLRA
TLDRVCHTIA KVAEEGSDQL VRQAGSALYH ITTAIFMAVE GVRLAPDHRR LALAYLVLRH
KLLPADPLAL PESDDALLFD ALVKQREVSF ALAMQALPDG GVQ
//