GenomeNet

Database: UniProt
Entry: A0A022QRB0_ERYGU
LinkDB: A0A022QRB0_ERYGU
Original site: A0A022QRB0_ERYGU 
ID   A0A022QRB0_ERYGU        Unreviewed;       676 AA.
AC   A0A022QRB0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   ORFNames=MIMGU_mgv1a002427mg {ECO:0000313|EMBL:EYU29818.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU29818.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU29818.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI631145; EYU29818.1; -; Genomic_DNA.
DR   RefSeq; XP_012846404.1; XM_012990950.1.
DR   AlphaFoldDB; A0A022QRB0; -.
DR   STRING; 4155.A0A022QRB0; -.
DR   GeneID; 105966392; -.
DR   KEGG; egt:105966392; -.
DR   eggNOG; KOG0135; Eukaryota.
DR   OMA; VMPNIQI; -.
DR   OrthoDB; 5473219at2759; -.
DR   PhylomeDB; A0A022QRB0; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
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   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:UP000030748}.
FT   DOMAIN          184..293
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          325..482
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          534..658
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        467
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   676 AA;  75703 MW;  D348E4827ACD645F CRC64;
     MEKFNFRTQV LIRHLQQTTA TATAAAISRS PCLSYAPPET SEPPSPFDVS SMRKLMDGHN
     LVDRDWVFNL MIQSKLFNPK MRGGKVFVVP DYNQSMEQQR EITMKRIQYL LDHGVFDGWL
     TGRGFESEMR KLALLEVIEI FDHSLAIKIG VHFFLWGGAI QFFGTKRHHD KWLSATENYL
     IKGCFSMTEL GHGSNVRGIE TVTTYDSKSG EFVINTPCES AQKYWIGGAA NHATHTVVFS
     QLNVDGKNEG VHAFITQIRD ADGNICPNIR IADCGHKIGL NGVDNGRIWF DNVRIPRENL
     LNSVADVSPD GKYLSAIKDP DQRFGAFMAP LTSGRVTIAA SAVYSAKISL AIAIRYSLTR
     RAFSITPDSA EVLLLDYPSH QHRLLPLLAK TYAMSFAANH LKLLYVKRTP QLIKTLHVVS
     SSFKAILTWH NMRTLQECRE ACGGQGLKTE NRIGQLKGEF DVQSTFEGDN NVLMQQVSKA
     LLGEYLAAKK RNKPFKDLGL DHMNKSCPTI PLQLTASTVR SVQFQNDILC LRERDLLNHF
     AAQVSKYQAQ GESKESAVIA SYRLAEDLGR AFSDRAIFQT FVEAENNVTD VPLKNILSVL
     RSMYVLVTLD EDAAFLRYGY LTVENAETVR KEVANLCSEM RPHALALVTS FGIPDAFLSP
     IAFDWIAANS WSPEQD
//
DBGET integrated database retrieval system