ID Q0KCN9_CUPNH Unreviewed; 420 AA.
AC Q0KCN9;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=FadE2-like Acyl-CoA dehydrogenase (ACAD) {ECO:0000313|EMBL:CAJ92232.1};
GN OrderedLocusNames=H16_A1091 {ECO:0000313|EMBL:CAJ92232.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ92232.1, ECO:0000313|Proteomes:UP000008210};
RN [1] {ECO:0000313|EMBL:CAJ92232.1, ECO:0000313|Proteomes:UP000008210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC 337 {ECO:0000313|Proteomes:UP000008210};
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ92232.1; -; Genomic_DNA.
DR RefSeq; WP_010809091.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0KCN9; -.
DR STRING; 381666.H16_A1091; -.
DR GeneID; 57643191; -.
DR KEGG; reh:H16_A1091; -.
DR PATRIC; fig|381666.6.peg.1475; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_1_2_4; -.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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:UP000008210}.
FT DOMAIN 10..133
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 137..234
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 250..398
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 420 AA; 46673 MW; 176B9B9C51937EBF CRC64;
MDFEYSPKVK EMQAKLLAFF DQHIYPNEKR FAAEIDANRR AGNAWVPTKV IEELKPLARA
AGLWNLFLPR SPRAPQGLSN LEYATLCEIM GRVPWSAEVF NCAAPDTGNM ETLERYASEE
LKDKWLEPLL AGEIRSAFLM TEPAVASSDA TNIECRIERD GDHYVINGTK WWSSGAGDPR
CKVYIVMGKT NPDAGRHEQQ SMIVVPADTP GITIKRFLPV FGYDDAPHGH MEIELKNVRV
PASNILLGEG RGFEIAQGRL GPGRIHHCMR SIGVAERALE LMCKRALSRV AFGKPVSSQG
VTQERIAEAR CEIEMARLLT LKAAYMMDTV GNKVAKAEIA MIKVIAPNVA LKVIDWAIQV
HGAAGVSSDF PLANWWAHQR TLRLADGPDE VHRNAIAKLE LAKHMNLNPD DIRMPVARGF
//
