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Database: UniProt
Entry: F4GDM7_ALIDK
LinkDB: F4GDM7_ALIDK
Original site: F4GDM7_ALIDK 
ID   F4GDM7_ALIDK            Unreviewed;       385 AA.
AC   F4GDM7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AEB82610.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:AEB82610.1};
GN   OrderedLocusNames=Alide2_0172 {ECO:0000313|EMBL:AEB82610.1};
OS   Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Alicycliphilus.
OX   NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB82610.1, ECO:0000313|Proteomes:UP000007938};
RN   [1] {ECO:0000313|EMBL:AEB82610.1, ECO:0000313|Proteomes:UP000007938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14773 / CIP 107495 / K601
RC   {ECO:0000313|Proteomes:UP000007938};
RX   PubMed=21742888; DOI=10.1128/JB.00365-11;
RA   Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA   van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA   Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA   Smidt H., Stams A.J.;
RT   "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL   J. Bacteriol. 193:5028-5029(2011).
RN   [2] {ECO:0000313|EMBL:AEB82610.1, ECO:0000313|Proteomes:UP000007938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14773 / CIP 107495 / K601
RC   {ECO:0000313|Proteomes:UP000007938};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA   Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT   "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL   Submitted (APR-2011) 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; CP002657; AEB82610.1; -; Genomic_DNA.
DR   RefSeq; WP_013517106.1; NC_015422.1.
DR   AlphaFoldDB; F4GDM7; -.
DR   STRING; 596154.Alide2_0172; -.
DR   KEGG; adk:Alide2_0172; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_1_4; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000007938; Chromosome.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; IPR006089; Acyl-CoA_DH_CS.
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; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEB82610.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007938}.
FT   DOMAIN          9..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   385 AA;  42071 MW;  2F5747608E9134FC CRC64;
     MIRDPEILEA LLDSVRRFVR ERLVPAENEV AETDEIPETI VQEMRELGLF GMTIPEKFGG
     LELTMEEECR VLLELCQTAP AFRSVIGTTV GIGSQGILMD GTPEQQAQWL PKLATGEVIA
     SFALTEPEAG SDAASLRTTA ILQGDHYVVN GTKRFITNAP HAGMFTLMAR TNPQDKGAGG
     VSSFIVDAKS PGISFGKYDK KMGQRGAHTC DVIFDNVKVP AANLIGLKEG QGFKTAMKVL
     EKGRIHIAAV AVGVAKRILR DALAYALERK QFGQPICEFQ LVQAMLADSQ AELYAAECMT
     IDAARRRDDG HNVSTEASCA KMFATEMCGR VADRAVQILG GAGYMAEYGI ERFYRDVRLF
     RLYEGTTQIQ QIIIARNMVR AARAA
//
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