Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9SS01 (AAE20_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Benzoate--CoA ligase, peroxisomal

EC=6.2.1.25
Alternative name(s):
Acyl-activating enzyme 20
Protein BENZOYLOXYGLUCOSINOLATE 1
Gene names
Name:AAE20
Synonyms:BZO1
Ordered Locus Names:At1g65880
ORF Names:F12P19.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Benzoate--CoA ligase involved in benzoyloxyglucosinolate biosynthesis in seeds. Glucosinolates are secondary metabolites involved in pathogen and insect defense of cruciferous plants. Ref.4

Catalytic activity

ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA. Ref.4

Subcellular location

Peroxisome Potential.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentPeroxisome
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: UniProtKB-KW

glucosinolate biosynthetic process

Inferred from mutant phenotype Ref.4. Source: TAIR

   Cellular_componentperoxisome

Inferred from sequence or structural similarity Ref.4. Source: TAIR

   Molecular_functionbenzoate-CoA ligase activity

Inferred from direct assay Ref.4. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Benzoate--CoA ligase, peroxisomal
PRO_0000415730

Regions

Motif578 – 5803Microbody targeting signal Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SS01 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3855327A59D6E3A7

FASTA58064,941
        10         20         30         40         50         60 
MDDLALCEAN NVPLTPMTFL KRASECYPNR TSIIYGKTRF TWPQTYDRCC RLAASLISLN 

        70         80         90        100        110        120 
ISKNDVVSVM APNTPALYEM HFAVPMAGAV LNPINTRLDA TSIAAILRHA KPKILFLDRS 

       130        140        150        160        170        180 
FEALARESLH LLSSEDSNLN LPVIFIHEND FPKRASFEEL DYECLIQRGE PTPSMVARMF 

       190        200        210        220        230        240 
RIQDEHDPIS LNYTSGTTAD PKGVVISHRG AYLCTLSAII GWEMGTCPVY LWTLPMFHCN 

       250        260        270        280        290        300 
GWTFTWGTAA RGGTSVCMRH VTAPEIYKNI EMHNVTHMCC VPTVFNILLK GNSLDLSPRS 

       310        320        330        340        350        360 
GPVHVLTGGS PPPAALVKKV QRLGFQVMHA YGQTEATGPI LFCEWQDEWN RLPENQQMEL 

       370        380        390        400        410        420 
KARQGISILG LADVDVKNKE TQKSAPRDGK TMGEILIKGS SIMKGYLKNP KATFEAFKHG 

       430        440        450        460        470        480 
WLNTGDVGVI HPDGHVEIKD RSKDIIISGG ENISSVEVEN VLYKYPKVLE TAVVAMPHPT 

       490        500        510        520        530        540 
WGETPCAFVV LEKSETTIKE DRVDKFQTRE RNLIEYCREN LPHFMCPRKV VFLEELPKNG 

       550        560        570        580 
NGKILKPKLR DIAKGLVVED EINVIAKEVK RPVGHFISRL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases."
Shockey J.M., Fulda M.S., Browse J.
Plant Physiol. 132:1065-1076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
[4]"Characterization of seed-specific benzoyloxyglucosinolate mutations in Arabidopsis thaliana."
Kliebenstein D.J., D'Auria J.C., Behere A.S., Kim J.H., Gunderson K.L., Breen J.N., Lee G., Gershenzon J., Last R.L., Jander G.
Plant J. 51:1062-1076(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC009513 Genomic DNA. Translation: AAF06049.1.
CP002684 Genomic DNA. Translation: AEE34436.1.
IPIIPI00544157.
PIRA96683.
RefSeqNP_176763.1. NM_105260.2.
UniGeneAt.35826.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ9SS01.
SMRQ9SS01. Positions 19-567.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G65880.1-P.

Proteomic databases

PRIDEQ9SS01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G65880.1; AT1G65880.1; AT1G65880.
GeneID842900.
KEGGath:AT1G65880.

Organism-specific databases

TAIRAt1g65880.

Phylogenomic databases

HOGENOMHOG000230005.
InParanoidQ9SS01.
OMALRHGECK.
PhylomeDBQ9SS01.
ProtClustDBPLN03102.

Enzyme and pathway databases

BioCycMetaCyc:AT1G65880-MONOMER.

Gene expression databases

GenevestigatorQ9SS01.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAAE20_ARATH
AccessionPrimary (citable) accession number: Q9SS01
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families