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Database: UniProt
Entry: A0A1W0BNU6_9NOCA
LinkDB: A0A1W0BNU6_9NOCA
Original site: A0A1W0BNU6_9NOCA 
ID   A0A1W0BNU6_9NOCA        Unreviewed;       741 AA.
AC   A0A1W0BNU6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ONM47647.1};
GN   ORFNames=B0T46_17310 {ECO:0000313|EMBL:ONM47647.1};
OS   Nocardia donostiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM47647.1, ECO:0000313|Proteomes:UP000188836};
RN   [1] {ECO:0000313|EMBL:ONM47647.1, ECO:0000313|Proteomes:UP000188836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1655 {ECO:0000313|EMBL:ONM47647.1,
RC   ECO:0000313|Proteomes:UP000188836};
RX   PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA   Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA   Potter G., Perez-Trallero E.;
RT   "Nocardia donostiensis sp. nov., isolated from human respiratory
RT   specimens.";
RL   Antonie Van Leeuwenhoek 109:653-660(2016).
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}.
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:ONM47647.1}.
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DR   EMBL; MUMY01000014; ONM47647.1; -; Genomic_DNA.
DR   RefSeq; WP_077118475.1; NZ_MUMY01000014.1.
DR   AlphaFoldDB; A0A1W0BNU6; -.
DR   STRING; 1538463.B0T36_09990; -.
DR   OrthoDB; 2431337at2; -.
DR   Proteomes; UP000188836; Unassembled WGS sequence.
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:SF4; ACYL-COA DEHYDROGENASE FADE34; 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   Reference proteome {ECO:0000313|Proteomes:UP000188836}.
FT   DOMAIN          6..84
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          232..349
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          392..483
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          488..582
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          594..733
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   741 AA;  77864 MW;  4D6C1B5EF732479A CRC64;
     MTIATTDEHK AVQESMRGWA AAVQPIATMR ADTTGFWRTY WPTLAELGIF RVAVAEDAGG
     ADGSVSDLAV LIERAAHDLV GGPVLATAVA GLVTGGSLDE TQPCGIALDT VAGPRSGGTG
     DADHDNAVGS ASSLATSEPG IETTDGELLL TGTWESVLGA APQTAVLLPV RFPDGRRWCL
     IPPDASGLQI EPLEPFDHST PLARVRCTDV PVAADAVFAP PYPVEDLIVA LAAAELAGIA
     GWCLDTAVDY AKVREQFGRK IGSFQAVKHI CAWMLCRTEL IRAVAADAAA AVDSGGAELP
     IAAAIAAAIA LDAAVDTAKD CIQVLGGIGF TWEHDAHFYL RRAVALRQLL GGAPHWRARV
     TELTRAGQRR STGADRVFEE TKGTETGGGA ADEELSAQVA RIAALPTDEQ RTALAEAGLL
     MPHWPKPYGR GADPMTGLVI SEELRRAGLE TPDLAIGGWA VPTLLQHGTQ EQIDRFAWAT
     LRGDVVWCQL FSEPEAGSDL AALRTTATKV DGGWALRGQK VWTSLANQAD WGICLARTDP
     DAPKHKGISY FLVDMRSKGI EIRPLVQITG EDRFSEVFLD EVFVPDDCVV GALGNGWRIA
     RSTLSTERVA MGGNGIGPVL EELIAKLPAT GAGAELVNDR LGGFVAEAIA GLLLEQRAAV
     RMLAGGDPGA QSSVRKLVGV RHRQAVAEFA VEVAGPAGAR ETEDTSEFLL TRCLSIAGGT
     EQILLTVAGE RILGLPREAG S
//
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