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Database: UniProt
Entry: A0A1D6ML15_MAIZE
LinkDB: A0A1D6ML15_MAIZE
Original site: A0A1D6ML15_MAIZE 
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}.
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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
//
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