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Database: UniProt
Entry: A0A1S1QK81_9ACTN
LinkDB: A0A1S1QK81_9ACTN
Original site: A0A1S1QK81_9ACTN 
ID   A0A1S1QK81_9ACTN        Unreviewed;       395 AA.
AC   A0A1S1QK81;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OHV33492.1};
GN   ORFNames=CC117_22785 {ECO:0000313|EMBL:OHV33492.1};
OS   Parafrankia colletiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV33492.1, ECO:0000313|Proteomes:UP000179627};
RN   [1] {ECO:0000313|Proteomes:UP000179627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA   Hurst S.;
RT   "Sequence Frankia sp. strain CcI1.17.";
RL   Submitted (JUL-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:OHV33492.1}.
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DR   EMBL; MBLM01000131; OHV33492.1; -; Genomic_DNA.
DR   RefSeq; WP_071087032.1; NZ_MBLM01000131.1.
DR   AlphaFoldDB; A0A1S1QK81; -.
DR   OrthoDB; 5167280at2; -.
DR   Proteomes; UP000179627; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179627}.
FT   DOMAIN          30..109
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          113..207
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          219..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   395 AA;  43489 MW;  F9DA4A96A5EA175D CRC64;
     MNDDLPEELH RRVERFLAAH DPATTERLTW LRARFDAGLA WVSFPAGLGG LGLPQALQAE
     VDGLFDDAGA PDNRKKANGI GLGMAAPTIL RFGTDAQKQR FLRPLWTGEE IWCQLFSEPG
     AGSDLAAVAT RAVRDGDTWV VSGQKVWTSG AHHARFAILL ARTNPDVPKH GGLTYFLCDM
     TDPGVDVRPL RQITGEAEFN EVFLTDVSIP DSHRLGAEGA GWKVANATLN NERVAIGGRA
     ALRESGMIGE VVDTWRTNPQ RRTPELHARL LGLWVEAEVA RLTGQRLRQK LALGQPGPEG
     ATMKLTFARL NQQLSGLELE LLGEDGLRYS DWSMTRPDKV DMTGRDAGYR YLRARGNSIE
     GGTSEILRNI IAERLLGLPA EPRVDKDIPW KELPR
//
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