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Database: UniProt
Entry: A0A3G8JN97_9ACTN
LinkDB: A0A3G8JN97_9ACTN
Original site: A0A3G8JN97_9ACTN 
ID   A0A3G8JN97_9ACTN        Unreviewed;       765 AA.
AC   A0A3G8JN97;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acyl-CoA dehydrogenase FadE17 {ECO:0000313|EMBL:AZG45929.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:AZG45929.1};
GN   ORFNames=D7316_02529 {ECO:0000313|EMBL:AZG45929.1};
OS   Gordonia insulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG45929.1, ECO:0000313|Proteomes:UP000271469};
RN   [1] {ECO:0000313|EMBL:AZG45929.1, ECO:0000313|Proteomes:UP000271469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG45929.1,
RC   ECO:0000313|Proteomes:UP000271469};
RA   Kim Y.S., Kim S.B.;
RT   "Gordonia insulae sp. nov., isolated from an island soil.";
RL   Submitted (NOV-2018) 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; CP033972; AZG45929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8JN97; -.
DR   KEGG; gom:D7316_02529; -.
DR   Proteomes; UP000271469; Chromosome.
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; 2.
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; 2.
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:SF3; ACYL-COA DEHYDROGENASE FADE29; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
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:AZG45929.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271469}.
FT   DOMAIN          48..120
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..384
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          410..493
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          624..754
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          386..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  81269 MW;  25DFEF21F225093D CRC64;
     MKRQETAVAV DDGIGDWRVR LTALLDDYRG RPRPTTSRDR LERSIAWQSE LVDAGLAAPG
     WPAAVGGMEL SLEDQLDYYR MTSGAGAPKH PCAMSFIVAP TIIVHGTQEQ RDRFLEPLLR
     ADEFWCQGFS EPGAGSDLAS LSTRAVRDGD SYRVTGQKVW TTKADRADWM FALVRTGPAG
     RSTSGITYLL IPMDAPGIEV RPLRDAAGGH HFAEIFFDDV VVPVVNRLGE EGEGWSIMRT
     SLGHERATAF LADEFRYRST VDKVLRLAVD RGYADDPLVR QELARVETSV RSITANSARA
     LDAVLRGGDP GGVASVNRLV KSEFEQHLHR LALRLTGNGA VLGARSAGVV ENGRWTYGYL
     MSRAATIGAG TSEIQRNTIA ESVLGLPSHR GEGTRPRTVV PGRPLTTPGD DESAIREALR
     GAIAARVDTS EVLGREGDPG GYDVALWRDL VAFGLPGLSA PEGLGGGGAP DRLLCAAVEE
     VAYHLAPVPL VPTAIALQLL LSCDPGETVE AVIAGVPAAF VVPIDDRGWS FDAWLPTLRG
     GRLDGAVDRV AGAPAAEVLV VAARDADTGE LRLVTVDPSV ASVTVQQSID LTATVGAVSF
     VDVPATVVAS GTAAVDALVF ARRHAQLLIA ADSVGVANRA LSLAVEWAGQ RQQFGQAIGS
     FQAISHKCAD LLVGAEGARG QVLAAADLAA SESDAAVAAD LACAEALSVA VRSGEECIQI
     HGGIGFTWEH PAHLLLRRAT ANEAWLVRPE VMRDRAVEEL VRRLR
//
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