ID A0A0D3GGF3_9ORYZ Unreviewed; 685 AA.
AC A0A0D3GGF3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART06G14280.2};
RN [1] {ECO:0000313|EnsemblPlants:OBART06G14280.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART06G14280.2};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART06G14280.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR AlphaFoldDB; A0A0D3GGF3; -.
DR EnsemblPlants; OBART06G14280.2; OBART06G14280.2; OBART06G14280.
DR Gramene; OBART06G14280.2; OBART06G14280.2; OBART06G14280.
DR Proteomes; UP000026960; Chromosome 6.
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; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 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, ECO:0000256|PIRNR:PIRNR000168};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960}.
FT DOMAIN 193..301
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 334..490
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 541..667
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 476
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 685 AA; 76295 MW; B3C682FF088C665C CRC64;
MSSSPAASRR AAAIARHLAG IPAAKFASLL EPFSCLGYVP PESNEQPPAF ALGDLRRLLD
GHDLGVRDWM FRVMEQSTLF CSRHGGPGPA GRVFASPDFN KDKEGQREAT MRRIGYLARR
GVFRGWLTDT EGDAEAELRR IALLDCIGVY DHSLAIKIGV HFFLWGSAIK FLGTKRHHDK
WLSDTENYVI KGCFSMTELG HGSNVRGIET VATYDIKTRE FVIYTPCESA QKYWIGGAAN
HATHTIVFAQ LHINGRNEGV HAFVAQIRDE HENVMPNIQI ADCGHKIGLN GVDNGRIWFN
NIRVPRENLL NLVADVLPDG QYVSTIDDPD QRFAAFLSPL TLGRVNIAVN AVYISKVGVA
IAVRYALSRR AFSVTPDGPE MLLLDYPSHQ RRLLPLLAKA CLMSSAGNFM KRMYVKRTPE
LNKSIHIYSS ALKATLTWQN MTTLQECREA CGGQGLKTEN RIGIFKAEFD VQSTFEGDNN
VLMQQVSKAL YAEFLTAKRK NQPFKGLGLE HLNGPCPVIP DYLTSGTLRS SSFQMDLLCL
RERDLLKRFT TEVSNYLAQG ESREKALMLS YQLAEDLARA FTERTILQIF LEDEKNIPTG
SLKDILGLLR SLYVMVCIDE SASFLRYGCL SRENVAAARK EVMTLCSELR PHALAIVSSF
GIPDAFLSPL AFDWIEANAR SSGNE
//
