ID E1VKF0_9GAMM Unreviewed; 389 AA.
AC E1VKF0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Long chain acyl coenzyme A dehydrogenase {ECO:0000313|EMBL:CBL45292.1};
GN Name=fadE {ECO:0000313|EMBL:CBL45292.1};
GN ORFNames=HDN1F_17090 {ECO:0000313|EMBL:CBL45292.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL45292.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL45292.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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; FP929140; CBL45292.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VKF0; -.
DR STRING; 83406.HDN1F_17090; -.
DR KEGG; gpb:HDN1F_17090; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_3_6; -.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000002677; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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 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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000002677}.
FT DOMAIN 18..129
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 133..229
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..388
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 389 AA; 43073 MW; 66F754468A7FECF3 CRC64;
MSSSAGYVAP MIPRTLFTEE HETFRKTVRR FFDEEITPFA DRWEEQQHID RNLWNKAGEL
GLLCPTMPEE YGGSGVDRLY STILMEEQAR SGDSASGFAL HSDIVANYIF NFGSEALKRH
WLPKMASGEA VAAIAMTEPG TGSDLQAVRT TAIADGDDYV INGSKIFITN GYLSDVVVVV
AKTGSGEKAA QNISLIVVEA SRAGFTKGKP LKKVGMRGQD TCELFFDNVR VPKTNLLGME
GMGFIMLMKE LAWERMMIAI ICAAGAEAVL ANTVDYVKQR KAFGKPISAF QNTRFKLAEM
RAEIQIARVY VDRCLELVLQ SKLSVEAAAS AKYWVSDLLS KVVDECVQLH GGYGYMLEYP
VARAYIDTRA NRIYGGTNEI MKELISRTI
//
