ID H1S8F0_9BURK Unreviewed; 579 AA.
AC H1S8F0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EHP41164.1};
GN ORFNames=OR16_21278 {ECO:0000313|EMBL:EHP41164.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP41164.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP41164.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP41164.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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:EHP41164.1}.
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DR EMBL; AHJE01000052; EHP41164.1; -; Genomic_DNA.
DR RefSeq; WP_006159704.1; NZ_AHJE01000052.1.
DR AlphaFoldDB; H1S8F0; -.
DR PATRIC; fig|1127483.3.peg.4255; -.
DR Proteomes; UP000005808; 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 3..163
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 170..275
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 286..442
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 579 AA; 62624 MW; 6C10485391443EEF CRC64;
MPDQHGVNLF ASDPDLRALL PLYLPPDLFA HLLPHLDRMG ALAGGVLDTL AHTADQNKPT
LSYRTRTGVD AQHIEKHPAY VELERVAFSE FGLAAASHRG GVLGWDKPMP AAAKYALTYL
FVQAEFGLCC PLSMTDSLTR TLRKFGDPAV VERFLPNLTT QVFEDLYQGA MFMTEQGAGS
DVAATTTRAA RDAQAEGGWR LSGDKWFCSN PDAALAMVLA RVEDENGEAA PGIKGVSLFL
LPRTLADGSA NHYRIIRLKD KLGTRSMASG EIRLEGAHAY LVGELGRGFV QMADMINNSR
LSNGVRAAGL MRRALSEGQF IARERRAFGK RLLDMPLMRR QLLKLALPTE QARTMVFQTA
EALRRADAGE ADAYPLMRVL TPLIKFRACR DARKVTGDAM EMRGGCGYIE EWSDPRLVRD
AHLGSIWEGT SNIVALDVLR AIRREGALPV LEAHLAGLLQ ATPMHAGARG AFTTAIARAT
TLAARAAEAG ADGDVLARQA ASGLYHVTSA AAMAWEAGRI GSVRRMRLAQ LVLLHRVLPQ
DPLAGQAEPD WLADTLDPTA PPADGAAHAA TAVEQVNLF
//