ID A0A1D6ML15_MAIZE Unreviewed; 451 AA.
AC A0A1D6ML15;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acyl-coenzyme A oxidase 4 peroxisomal {ECO:0000313|EMBL:ONM29902.1};
GN ORFNames=ZEAMMB73_Zm00001d039768 {ECO:0000313|EMBL:ONM29902.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM29902.1};
RN [1] {ECO:0000313|EMBL:ONM29902.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM29902.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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; CM007649; ONM29902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6ML15; -.
DR SMR; A0A1D6ML15; -.
DR IntAct; A0A1D6ML15; 2.
DR STRING; 4577.A0A1D6ML15; -.
DR InParanoid; A0A1D6ML15; -.
DR ExpressionAtlas; A0A1D6ML15; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
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; 1.
DR InterPro; IPR045008; ACX4-like.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR PANTHER; PTHR43188:SF11; OS01G0159400 PROTEIN; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 69..178
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 184..276
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 293..433
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 451 AA; 48723 MW; FED99BAFA1134237 CRC64;
MAGKRGRSAF LPSFLCWARL VTGRDGQDEG GAKAGLPAMD ISLAFPQATP ASIFPPSASD
YYQSDDLLTS EERSIRMKVR GIMEKEIAPI MSAYWEKAEF PFNAIPKLAS LGVAGGTIKG
YGCPGLSITA SAVTMSEIAR VDASCSTFIL VHSSLAMVTI ALCGSEAQKQ KYLPSLAQLT
TVGCWALTEP NYGSDASSLR TIATKAPGGW HIDGQKRWIG NSTFADVLVV LARNADTQQL
NGFIVRKGAP GLKATKIENK IGLRMVQNGD IVLNKVFVPD EDRLPGINSF QDISKVLAIS
RIMVAWQPVG ISMGVFDMCH RYLKERKQFG VPLAAFQLNQ EKLARMLGNV QSMVLVGWRL
CKLYESGKMT PGHASLGKAW NSRTAREVVS LGRELLGGNG ILADFLVAKA FCDLEPIYSY
EGTYDINSLV TGREVTGIAS FRPAAPAKAR L
//