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Database: UniProt
Entry: C5C2W6_BEUC1
LinkDB: C5C2W6_BEUC1
Original site: C5C2W6_BEUC1 
ID   C5C2W6_BEUC1            Unreviewed;       694 AA.
AC   C5C2W6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Acyl-CoA oxidase domain protein {ECO:0000313|EMBL:ACQ81810.1};
GN   OrderedLocusNames=Bcav_3568 {ECO:0000313|EMBL:ACQ81810.1};
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Beutenbergia.
OX   NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ81810.1, ECO:0000313|Proteomes:UP000007962};
RN   [1] {ECO:0000313|EMBL:ACQ81810.1, ECO:0000313|Proteomes:UP000007962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC   {ECO:0000313|Proteomes:UP000007962};
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; CP001618; ACQ81810.1; -; Genomic_DNA.
DR   RefSeq; WP_015884047.1; NC_012669.1.
DR   AlphaFoldDB; C5C2W6; -.
DR   STRING; 471853.Bcav_3568; -.
DR   KEGG; bcv:Bcav_3568; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_014629_4_0_11; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000007962; 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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
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   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:UP000007962}.
FT   DOMAIN          138..217
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          508..650
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   REGION          670..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  75684 MW;  F96C9441406C098F CRC64;
     MTTTLPTNAR IDVGALADLL DGRWADIRRR TRNLALEPRY RRTLGLSMAE HRARVREQAQ
     ALADSGEVQR AFPSRLGGAD NPGGNIAGFE ELVVADPSLQ IKAGVQWGLF GAAVLHLGTA
     YHHEEFLPGI MSMAVPGCFA MTETGHGSDV ASIGTTATYD ADAEEFVIHT PTRSAWKEYI
     GNAAVDGVAA VVFAQLVTRG VDHGVHAFYV PLRDTAGERD EHGAYPYLPG VGGEDDGLKG
     GLLGVDNGRL HFDQVRIPRR NLLDKYAEVA ADGEYSSPID SPGRRFFTML GTLVQGRVSL
     GGSSVATSKI ALSTAIRYGN ERRQFTTSDP HTESVILDYG AHQRRLLPLL ARTYAAAFLH
     DTLLERFHGV FSGEHETDAD REDLETLAAA SKALSTWLAL DVVQTSREAC GGAGYMAENG
     LVGLHQDMDV YVTFEGDNTV LLQLVGKRLL TDYGREMATM DVAGAVRYVA DRAGDMALHR
     TPLRRASQSI RDWGSRARSA EELREPATQR ELLEDRVEAM VEVIAGKLRA VQKASAAEQA
     AAFNAHQHEL IEAARAHGEL MQWEAFTAGI ARTSDPTTKQ VLTWLRDLFG LATIEKNLAW
     YLVNGRLSAQ RARTVTSYIE RLLVRLRPHA EDLVDAFGYS AELIGAPIGT GAEGERQDEA
     QAYYRELRAS GQEPVTEKAL RAREKKAARA ARAS
//
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