ID   AAE20_ARATH             Reviewed;         580 AA.
AC   Q9SS01;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 142.
DE   RecName: Full=Benzoate--CoA ligase, peroxisomal;
DE            EC=6.2.1.25;
DE   AltName: Full=Acyl-activating enzyme 20;
DE   AltName: Full=Protein BENZOYLOXYGLUCOSINOLATE 1;
GN   Name=AAE20; Synonyms=BZO1; OrderedLocusNames=At1g65880;
GN   ORFNames=F12P19.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY.
RX   PubMed=12805634; DOI=10.1104/pp.103.020552;
RA   Shockey J.M., Fulda M.S., Browse J.;
RT   "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT   Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT   a synthetases.";
RL   Plant Physiol. 132:1065-1076(2003).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17651367; DOI=10.1111/j.1365-313x.2007.03205.x;
RA   Kliebenstein D.J., D'Auria J.C., Behere A.S., Kim J.H., Gunderson K.L.,
RA   Breen J.N., Lee G., Gershenzon J., Last R.L., Jander G.;
RT   "Characterization of seed-specific benzoyloxyglucosinolate mutations in
RT   Arabidopsis thaliana.";
RL   Plant J. 51:1062-1076(2007).
CC   -!- FUNCTION: Benzoate--CoA ligase involved in benzoyloxyglucosinolate
CC       biosynthesis in seeds. Glucosinolates are secondary metabolites
CC       involved in pathogen and insect defense of cruciferous plants.
CC       {ECO:0000269|PubMed:17651367}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzoate + ATP + CoA = benzoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC         ChEBI:CHEBI:456215; EC=6.2.1.25;
CC         Evidence={ECO:0000269|PubMed:17651367};
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AC009513; AAF06049.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34436.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7032226.1; -; Genomic_DNA.
DR   PIR; A96683; A96683.
DR   RefSeq; NP_176763.1; NM_105260.3.
DR   AlphaFoldDB; Q9SS01; -.
DR   SMR; Q9SS01; -.
DR   FunCoup; Q9SS01; 138.
DR   STRING; 3702.Q9SS01; -.
DR   GlyGen; Q9SS01; 2 sites.
DR   iPTMnet; Q9SS01; -.
DR   PaxDb; 3702-Q9SS01; -.
DR   ProteomicsDB; 244624; -.
DR   GeneID; 842900; -.
DR   KEGG; ath:AT1G65880; -.
DR   Araport; AT1G65880; -.
DR   TAIR; AT1G65880; BZO1.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_5_1; -.
DR   InParanoid; Q9SS01; -.
DR   OMA; IRLMYTS; -.
DR   PhylomeDB; Q9SS01; -.
DR   BioCyc; ARA:AT1G65880-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G65880-MONOMER; -.
DR   PRO; PR:Q9SS01; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   GO; GO:0009507; C:chloroplast; ISM:TAIR.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0018858; F:benzoate-CoA ligase activity; IDA:TAIR.
DR   GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR   CDD; cd12118; ttLC_FACS_AEE21_like; 1.
DR   FunFam; 3.30.300.30:FF:000008; 2,3-dihydroxybenzoate-AMP ligase; 1.
DR   FunFam; 3.40.50.12780:FF:000003; Long-chain-fatty-acid--CoA ligase FadD; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR045851; AMP-b_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR000873; AMP-dep_synth/lig_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   NCBIfam; NF006020; PRK08162.1; 1.
DR   PANTHER; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR43859:SF25; BENZOATE--COA LIGASE, PEROXISOMAL-RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE   1: Evidence at protein level;
KW   Ligase; Peroxisome; Plant defense; Reference proteome.
FT   CHAIN           1..580
FT                   /note="Benzoate--CoA ligase, peroxisomal"
FT                   /id="PRO_0000415730"
FT   MOTIF           578..580
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   580 AA;  64941 MW;  3855327A59D6E3A7 CRC64;
     MDDLALCEAN NVPLTPMTFL KRASECYPNR TSIIYGKTRF TWPQTYDRCC RLAASLISLN
     ISKNDVVSVM APNTPALYEM HFAVPMAGAV LNPINTRLDA TSIAAILRHA KPKILFLDRS
     FEALARESLH LLSSEDSNLN LPVIFIHEND FPKRASFEEL DYECLIQRGE PTPSMVARMF
     RIQDEHDPIS LNYTSGTTAD PKGVVISHRG AYLCTLSAII GWEMGTCPVY LWTLPMFHCN
     GWTFTWGTAA RGGTSVCMRH VTAPEIYKNI EMHNVTHMCC VPTVFNILLK GNSLDLSPRS
     GPVHVLTGGS PPPAALVKKV QRLGFQVMHA YGQTEATGPI LFCEWQDEWN RLPENQQMEL
     KARQGISILG LADVDVKNKE TQKSAPRDGK TMGEILIKGS SIMKGYLKNP KATFEAFKHG
     WLNTGDVGVI HPDGHVEIKD RSKDIIISGG ENISSVEVEN VLYKYPKVLE TAVVAMPHPT
     WGETPCAFVV LEKSETTIKE DRVDKFQTRE RNLIEYCREN LPHFMCPRKV VFLEELPKNG
     NGKILKPKLR DIAKGLVVED EINVIAKEVK RPVGHFISRL
//