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Database: UniProt
Entry: A0A1M7J943_9ACTN
LinkDB: A0A1M7J943_9ACTN
Original site: A0A1M7J943_9ACTN 
ID   A0A1M7J943_9ACTN        Unreviewed;       395 AA.
AC   A0A1M7J943;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SHM49526.1};
GN   ORFNames=SAMN05216499_111168 {ECO:0000313|EMBL:SHM49526.1};
OS   Actinacidiphila paucisporea.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310782 {ECO:0000313|EMBL:SHM49526.1, ECO:0000313|Proteomes:UP000184111};
RN   [1] {ECO:0000313|EMBL:SHM49526.1, ECO:0000313|Proteomes:UP000184111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHM49526.1,
RC   ECO:0000313|Proteomes:UP000184111};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FRBI01000011; SHM49526.1; -; Genomic_DNA.
DR   RefSeq; WP_073499797.1; NZ_FRBI01000011.1.
DR   AlphaFoldDB; A0A1M7J943; -.
DR   STRING; 310782.SAMN05216499_111168; -.
DR   OrthoDB; 3964153at2; -.
DR   Proteomes; UP000184111; 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:UP000184111}.
FT   DOMAIN          12..108
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          112..196
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          218..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   395 AA;  43035 MW;  14B3F2E454ADBFEC CRC64;
     MGSVSAADVR GRVRALLAAW DQKADPAEFL RARFDAGLAW VHFPVGLGGL DAPRALQAVV
     NAELDAAGAP DNDPRRIGIG LGMAAPTILA YGTDEQKARF LRPLWTGEEV WCQLFSEPGA
     GSDLAGLGTR AVRDGDDWVV DGQKVWTSSA HTARWAILIA RTDLDVPKHR GITYFVCDMT
     DPGVEVRPLR QITGEAEFNE VFLTGVRIPD AHRLGAVGDG WRVAQATLMN ERVAIGGGAS
     VPRESGMIGP VAATWRERPE LRTPELHDRL LRLWVDSEVA RLTAERVRQQ MAAGTPGPEG
     SGLKLSLARL NQQLSGLEVE LLGEQGLRYG DWAMVRPRSV DFYGRDAGYR YLRAKGNSIE
     GGTSEILRNI VAERVLGLPA EPRNDKDAAW KDLPR
//
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