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Entry: G2NK98_STREK
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ID   G2NK98_STREK            Unreviewed;       653 AA.
AC   G2NK98;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Acyl-CoA oxidase domain protein {ECO:0000313|EMBL:AEN08522.1};
GN   ORFNames=SACTE_0582 {ECO:0000313|EMBL:AEN08522.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN08522.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN08522.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN08522.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
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   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; CP002993; AEN08522.1; -; Genomic_DNA.
DR   RefSeq; WP_014044514.1; NC_015953.1.
DR   AlphaFoldDB; G2NK98; -.
DR   STRING; 862751.SACTE_0582; -.
DR   KEGG; ssx:SACTE_0582; -.
DR   PATRIC; fig|862751.12.peg.624; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_014629_4_0_11; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; 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; 2.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR012258; Acyl-CoA_oxidase.
DR   InterPro; IPR002655; Acyl-CoA_oxidase_C.
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; PTHR10909:SF382; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 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   PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397}.
FT   DOMAIN          34..142
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          147..255
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          289..450
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          510..649
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   653 AA;  71238 MW;  E3C7420CA365D846 CRC64;
     MATDNAHTAT SGYVEPEVDV RALTEVLDGE YAEIRDLVRT NLVTYASVLE EAEELGVDAY
     RERVRELVVE MAATGQTGMG FPGRYGGGGD IGASIAAFET LAFGDLSVLV KVGVQFGLFG
     GAILQLGTER HHDAYLPDLI TGRLMGCFAM TETGHGSNVQ ALGTLARYDA EGQEFVITTQ
     GDQARKDYIG NAARHAELAV VFAQLEVAGK SEGVHAFVVP IRVDGEVAPG VRIEDDGRKM
     GLNGVDNGRI RFDGVRVPRE ALLNRFADVT AEGVYESSID NPDRRFFTML GTLVQGRVSV
     GGAGVNAAKV ALAIATKYAV RRRQFEAASG AEEQRLLDYG LHQRRLLPLV ARTYALHFAQ
     DVVRTQLHEV FSGIEDDAQA RRRLESRAAG TKALGTWHAT RVVQECREAC GGAGYLSVNR
     FAALKADSDI FTTFEGDNHV LLQLVAKGLL THYASEFEDL DQLGTVRYVA GLAVETVMEK
     TSAHKLLERV RDLLPGGDEW DQEAGLLDSE YQLAMLRYRE EHMLAGVARR LKRGVDQKGN
     PGVVFSQVQD HVIAVAHAHV ERLVLEAFVE KVRALPDSGN KVALGLLCDL FALSTIEADR
     AWFMEHGRLT VQRSKAISRE VNDLCRKVRP LAVDLVDAWG IPSEMLRAPD LVG
//
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