ID J7S4E5_KAZNA Unreviewed; 750 AA.
AC J7S4E5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN Name=KNAG0B00630 {ECO:0000313|EMBL:CCK68511.1};
GN OrderedLocusNames=KNAG_0B00630 {ECO:0000313|EMBL:CCK68511.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK68511.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK68511.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001201};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00004846}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR EMBL; HE978315; CCK68511.1; -; Genomic_DNA.
DR AlphaFoldDB; J7S4E5; -.
DR STRING; 1071383.J7S4E5; -.
DR eggNOG; KOG0136; Eukaryota.
DR HOGENOM; CLU_014629_3_1_1; -.
DR OMA; ICTRFSA; -.
DR OrthoDB; 5777at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000006310; Chromosome 2.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
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; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF14749; Acyl-CoA_ox_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|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310}.
FT DOMAIN 31..171
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 184..294
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 548..726
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 488
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 750 AA; 84580 MW; E21B82143FABD4D9 CRC64;
MTRVSSTDTS QPVFEPVRLL RTERERSQLK TDEINTFLES SPEQRQLTHE LIDQIVNDPV
LKCDTGYYEQ EKLQERENTV KKIARLALYM EEDIKTVRQH FKGTDLFQSL QEDSGSLPPL
SNKDLSIFDK RLSLLANIDP QLSTRVGVHL GLFGNCIKGN GTDEQIKYWL QERGAVLLKG
IYGCFAMTEL GHGSNVANLQ TRATYNQNTD TFTINTPDLT ATKWWIGGAA HSATHSAVYA
RLIVKGKDYG VKTFVVPLRD PVNFQLLPGI TIGDIGKKMG RDGIDNGWIQ FRNVVIPREY
MLSRFAKVTP TEDGKDVQVN IEPQLDQISG YSALLSGRVN MVMDSFRFGS KFVTIATRYS
VGRQQFASTK GAEESQLIDY SLHQYRVLPQ LAIAYMVSPA AFNLMSTYYS TLDELYSVSS
NKNDKGLKTV SAKLKNLFIS SASLKATNTW LVANLIDELR QCCGGHGYSQ YNGFGKGYND
WVVQCTWEGD NNILSLTSAK SILKKFVDAA TKGKFDEELD SDLFDYLDPN FIRQVYTHEA
EADLVDDDLS SYVEVWSIAL VSLLVHIGKT IQKTKDFERI TKLLILVSKF HAFHTMLKAY
YEKLSDNASP VKDEATKEAL WDVFKLYSVY FIDKFSGEFQ QFKIFTPSQI TTLVQPKLLE
LLPKIRQNCI ALTDAFELPD QMLNAPIGYF DGDIYHNYFN EVVKNNPTEP DGAGKPPYHA
MLTTMLSRGY ETDERLGGSS STSVLEKLGK
//
