ID   A0A1B6ZES8_9SPHN        Unreviewed;       583 AA.
AC   A0A1B6ZES8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OAO05148.1};
GN   ORFNames=A8B75_04960 {ECO:0000313|EMBL:OAO05148.1};
OS   Sphingomonadales bacterium EhC05.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1849171 {ECO:0000313|EMBL:OAO05148.1, ECO:0000313|Proteomes:UP000078455};
RN   [1] {ECO:0000313|Proteomes:UP000078455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC05 {ECO:0000313|Proteomes:UP000078455};
RA   Rosana A., Orata F., Boucher Y., Case R.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OAO05148.1}.
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DR   EMBL; LXYP01000002; OAO05148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6ZES8; -.
DR   STRING; 1849171.A8B75_04960; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000078455; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 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, 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:UP000078455}.
FT   DOMAIN          74..155
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..270
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          289..448
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          484..576
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   583 AA;  62007 MW;  02903F98D3205626 CRC64;
     MTFTAPSREQ NFVLKHIAEI GELAQHDRFA GASEDMVEAI VEGIGQFAMG EFAPLNRIGD
     TVGAKWSDGA VTTPTGFQEA YQQFVEGGWA SIDGPEAFGG QDLPYSLSAL ILETCGAANF
     AFTLCPMLSF GAIEAIHAHG SDEQKAKYLP NLISGAWTGT MNLTEPQAGS DVGALRSTAE
     PITEGEHAGK YRIKGQKIYI TFGEHDLTDN IVHLVLARTP GAPEGTRGIS LFIVPKYHLD
     ADGKSGAAND VTCVSIEHKI GIHGSPTCVM AYGEQDECIG EMIGGEFGGI KAMFTMMNNA
     RINVGSQGVQ IGERATQQAL YFAMDRVQSA RAGSGNKNPV AIIEHPDVRR MLLRSKALTQ
     AARALLYYAT SSVDRATLGI EGAKSRAEIL TPLIKGYGTD IGNEVASIGV QIHGGMGFIE
     ETGAGQHFRD ARIAPIYEGT NGIQAADLVG RKLGLDGGEA LKTLISDIKA GAQDDDGLMI
     LAMACEDIAN WMACGEASID DRLAGSYPFM TMLATATCGM LMAKQYRIAE AELSNGDDPF
     LEAKLVTTRY YLDHLVPEAM GLKAAAMAGA DLLYRLSSDQ LVA
//