ID K3XV57_SETIT Unreviewed; 908 AA.
AC K3XV57;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0008006|Google:ProtNLM};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL10641, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQL10641, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL10641,
RC ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQL10641}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL10641};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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}.
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DR EMBL; AGNK02002459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3XV57; -.
DR STRING; 4555.K3XV57; -.
DR EnsemblPlants; KQL10641; KQL10641; SETIT_005814mg.
DR Gramene; KQL10641; KQL10641; SETIT_005814mg.
DR eggNOG; KOG0135; Eukaryota.
DR HOGENOM; CLU_014629_4_0_1; -.
DR InParanoid; K3XV57; -.
DR OMA; WKLPGCF; -.
DR Proteomes; UP000004995; Chromosome IV.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
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 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:UP000004995}.
FT DOMAIN 416..524
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 557..713
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 758..890
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 32..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 99383 MW; 9CC94C0CEDFD9699 CRC64;
MRWGTDLASE LKPLVVGRSK TPAMGDGPFL LVNAMGNGPH RRTGTTRSRA GQRCRPRGTR
PRPGTARPRR RGPGTTSPRR ATSPPPAATL YRRWFGTCAG TGTAAAATPL APPPIHSHRP
HTRLLAARPR SLPAAARPLR RPAPPLRPSL LSAAPPCLLP PPPAPAGSGS GVGRGSEGGG
MCRPATIISL TPLFPHFSTE LPSLQYLDCG SSHHDPNSPT AMDPALSPAG RRAATIARHL
AGALPSPPPL AATVALLGPS PCLSYALPES TEPAPAFPPA ELRALLDGHH LWERDWVFRV
MEESQLFCPR QRCSGSRVFV APDYNDGKEA QREATMRRVA HLARRGVFRG WLTEPGAEAE
LRKLALLESL GVYDHSLAIK IGVHFFLWGS AIKFLGTKRH HDKWLFATEN YDIKGCFAMT
ELGHGSNVRG IETIATYDSK AREFIINTPC ESAQKYWIGG AANHATHTIV FSQLHINGKN
EGVHAFVAQI RDGDGNVLPN IHIADCGHKI GLNGVDNGRI WFQNIRVPRE NLLNWVADVL
PDGQYVSMID DQDQRFAAFL SPLTLGRVNI AVNSVYISKV GLAIAVRYGL SRRAFSLTPD
GPEMLLLDYP SHQRRLLPLL AKVCLMSSAG NFMKKMYVKR TPEMSKAIHI YSSALKATLT
WQNMITLQEC REACGGQGLK TENRVGIFKA EFDVQSTFEG DNNVLMQQVS KALYAEFLAA
QKKKKPFKGL GLEHLNGPSP VIPDKLTGSI LRSSKFQMDL FCLRERDLLK QFAEEVSLHL
ARGESREKAL MLSFQLAEDL ARAFTERTIL QIFLEDEMNV PSGSLKELLG LLRSLYVMVS
IDESASFLRY GYLSRGNVAG VRKEVLKLCS ELRPHALAVV SSFGIPDAFL SPLAFDWIEA
NALSTGSH
//
