ID A0A197K7D5_9FUNG Unreviewed; 681 AA.
AC A0A197K7D5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=K457DRAFT_69144 {ECO:0000313|EMBL:OAQ33400.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ33400.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ33400.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ33400.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) 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; KV442021; OAQ33400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197K7D5; -.
DR STRING; 1314771.A0A197K7D5; -.
DR OrthoDB; 5777at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
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:UP000078512}.
FT DOMAIN 14..124
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 136..246
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 488..652
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 681 AA; 76880 MW; D29BF7F4AFCFF048 CRC64;
MESMTEERQK ATFDVRELTY FLDGGEKYTK IREKFMMELE RDPTFRMYDM YDVTKDQIRE
RTMEKFRTIV HYVSAEPVPI FTMRMQTISL IDPGFWTRFG VHYGLFFGAL RGSATSAQFS
HWVSKGALAL NGMVGCFAMT ELGHGSNVAG LETTATFDEA SDQFIIHTPT ITATKWWIGG
AAHTATHTVV FAQLIVRGKR YGTKSFVVQL RDTHTYKLMP GINIGDIGKK MGRDGIDNGW
IQFTNVRIPR TNMLMKHTKV SRAGEVKEPP MAQLTYGALI QGRVAMVVDS GNIAKKAVTI
AGRYAAVRRQ FSSNPHDVQE TKLIDYAIHQ YRLMPLLAQA YAFHFTGVET NKLYDDLMDK
LESTQPDDET MGEVIDTLKE THATSAGLKA FCTWSTLNAI EACRQTLGGH GYSAYTGLAT
TYNDFAVHCT WEGDNTILTL QSGRYLVSCY REALAGKSQP EGVSYLNHLD SLLNLGCGVK
TNEEILNFDV IQEAWGVVTA NVVKKAGDDF EVSLKAGMSP EAAYEECSQA RLAAAKIHSY
GYIFRRFAQA VKSAPEKLQA VLTKLCLLYG LYSIEQNAGF FLQYRYFTPS QMDYVRGQVN
VFCREVRQEY IPLIDAFNYS DYMINSPLGV YDGNIYEKYF DQVKRQNPVG GEHPYLPLIQ
SLLRRNIEDD EPLEDDDEDD E
//
