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Database: UniProt
Entry: U5E6R9_NOCAS
LinkDB: U5E6R9_NOCAS
Original site: U5E6R9_NOCAS 
ID   U5E6R9_NOCAS            Unreviewed;       583 AA.
AC   U5E6R9;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Acyl-CoA dehydrogenase/oxidase C-terminal domain-containing protein {ECO:0000259|Pfam:PF00441};
GN   ORFNames=NCAST_05_04750 {ECO:0000313|EMBL:GAD82038.1};
OS   Nocardia asteroides NBRC 15531.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD82038.1, ECO:0000313|Proteomes:UP000017048};
RN   [1] {ECO:0000313|EMBL:GAD82038.1, ECO:0000313|Proteomes:UP000017048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD82038.1,
RC   ECO:0000313|Proteomes:UP000017048};
RX   PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA   Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA   Suzuki K., Fujita N., Gonoi T.;
RT   "Genome based analysis of type-I polyketide synthase and nonribosomal
RT   peptide synthetase gene clusters in seven strains of five representative
RT   Nocardia species.";
RL   BMC Genomics 15:323-323(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:GAD82038.1}.
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DR   EMBL; BAFO02000005; GAD82038.1; -; Genomic_DNA.
DR   RefSeq; WP_019048107.1; NZ_VBUS01000004.1.
DR   AlphaFoldDB; U5E6R9; -.
DR   STRING; 1824.SAMN05444423_106196; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 5427839at2; -.
DR   Proteomes; UP000017048; 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; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF19; ACYL-COA DEHYDROGENASE FADE4-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017048}.
FT   DOMAIN          253..402
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   583 AA;  64979 MW;  5610516B1FF0271D CRC64;
     MTSSPSLLFN PATYDPQHFD AETRRLLRAT IEWFESKGKA QLLAEDRDAV WTQEFLDFVA
     KEKLFATFLT PAAYADGDPN KRWDAARNAA LAEIFGFYGL AYWYAEQVTI LGLGPIWQSD
     NEIAKRKAAA DLDAGQVMAF ALSEREHGAD IYNTDLILTP SEPGSADAEA GILFRANGEK
     YYIGNGNVAS MVSVFSRRGD VEGPEGYIWF AADSRHENYH LVESVIHGQM YVSHFRLENY
     PVTAADVLHE GPEGFSAALN TVNVGKFNLC HGSIGMVEHS FFEAITHANN RILYGNPVTD
     FGHVRGNFVD AYARLIAMKL FSDRAVDYFR SASLEDRRYL LFNPMTKSKV TSEGEVAMTL
     LLDVLAAKGF EKATYFAQAS RYINHLPRLE GTVHVNVGQI LKFMPNYLLN PAEYPAIGTD
     LVPGDQEFFW KQGPARGAGK VQFADWTPAY EQAADVPNVG RFYEQAQALR TLLLTAAPDA
     AQQKDLDFML TIGHLFSTVV YGQLILEQAE LTGLDRDVLD QIFDFQIRDF NTHATALLGK
     PSVTEGQREW AIGALRSPVA DTARFDRVWQ QVASYDGAYA MRP
//
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