ID A0A0M4QLV8_9PSEU Unreviewed; 656 AA.
AC A0A0M4QLV8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:ALE86152.1};
GN ORFNames=XF36_25955 {ECO:0000313|EMBL:ALE86152.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE86152.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE86152.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE86152.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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; CP011868; ALE86152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4QLV8; -.
DR KEGG; pseh:XF36_25955; -.
DR PATRIC; fig|1641402.3.peg.5561; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000062082; 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; 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; 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 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:UP000062082}.
FT DOMAIN 135..244
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 278..440
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 496..630
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 656 AA; 71294 MW; 5F324C66E8E0AA5B CRC64;
MPTPDRIPAE TLRTVVDGRW AHVRQQTREQ LAANADMRAD PDLSSADYRG RITDSLKFLT
SSGRPHTGFD PSVGGEGDVG GVVTAFAMLA YGDLSLLVKA GVQWGLFGGA VQVLGTERHH
EQYLRKIIDG ELLGCFAMTE SGHGSDVQHL HTTATYDAAA GEFVLHTPYP QARKEYIGNA
ARDGRMAVVF AQLVTGDEKP GVHAFLVPLR DSDGNALPGV TIGDDGRKAG LNGVDNGRLT
FDHVRIPREN LLNRFADVAP DGTYSSSIEN ETARFFTMLG TLVRGRISVA GGAGGAAQKA
LALAVRFGER RRQFANPATG EETTVLDYLA HQQKLLPALA TTFALHFTQD DLVKRMHDVQ
APGAGPVGAR EQRTLEQSAA GIKAIATWHA THTIQTCREA CGGAGYLEEN LLPALKADTD
VFTTFEGDNT VLLQLLAKEL LSDYGRTIKK GNPLEIAPLL GRQLAGVLAE RTGAASLTRR
IPFRGIDLTD RRRRRELLEV RRADTLAAAI RNLAPAMRKG NDEFTVFNSA QDLLLVAARA
HVDTLVERSF ADKLATIDDP AVRALLERVY DLHVLSVIDR ERAWYLETGR LTAAESRSIR
PLVNGLCREL RPYARTLVDG FGIPDEWLAC PMLDDEAWAP APGRPAEPLT EQVEAG
//
