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Q84P23 (4CLL9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 48. 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:
4-coumarate--CoA ligase-like 9

EC=6.2.1.-
Alternative name(s):
4-coumarate--CoA ligase isoform 4
Short name=At4CL4
Gene names
Name:4CLL9
Ordered Locus Names:At5g63380
ORF Names:K9H21.11, K9H21.8
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Converts 12-oxo-phytodienoic acid (OPDA) into OPDA-CoA. Ref.8

Subcellular location

Peroxisome Ref.8.

Domain

Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity By similarity.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=11 µM for OPDA

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
Oxylipin biosynthesis
   Cellular componentPeroxisome
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processjasmonic acid biosynthetic process

Inferred from direct assay Ref.8. Source: TAIR

   Cellular componentperoxisome

Inferred from direct assay Ref.8. Source: TAIR

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fatty-acyl-CoA synthase activity

Inferred from direct assay Ref.8. Source: TAIR

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5625624-coumarate--CoA ligase-like 9
PRO_0000299182

Regions

Nucleotide binding212 – 2209ATP By similarity
Nucleotide binding353 – 3586ATP By similarity
Region283 – 35270SBD1 By similarity
Region353 – 41765SBD2 By similarity
Motif560 – 5623Microbody targeting signal Potential

Sites

Binding site4381ATP By similarity
Binding site4531ATP By similarity
Binding site5441ATP By similarity

Experimental info

Sequence conflict5231T → A in AAP03018. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q84P23 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: DE8E87063F2B2DB3

FASTA56261,278
        10         20         30         40         50         60 
MLTKTNDSRL IDRSSGFDQR TGIYHSLRPS LSLPPIDQPL SAAEFALSLL LKSSPPATAG 

        70         80         90        100        110        120 
KNIEALTYLV NSSSGDNLTY GELLRRVRSL AVSLRERFPS LASRNVAFIL SPSSLDIPVL 

       130        140        150        160        170        180 
YLALMSIGVV VSPANPIGSE SEVSHQVEVS EPVIAFATSQ TVKKLQSSSL PLGTVLMDST 

       190        200        210        220        230        240 
EFLSWLNRSD SSSVNPFQVQ VNQSDPAAIL FSSGTTGRVK GVLLTHRNLI ASTAVSHQRT 

       250        260        270        280        290        300 
LQDPVNYDRV GLFSLPLFHV FGFMMMIRAI SLGETLVLLG RFELEAMFKA VEKYKVTGMP 

       310        320        330        340        350        360 
VSPPLIVALV KSELTKKYDL RSLRSLGCGG APLGKDIAER FKQKFPDVDI VQGYGLTESS 

       370        380        390        400        410        420 
GPAASTFGPE EMVKYGSVGR ISENMEAKIV DPSTGESLPP GKTGELWLRG PVIMKGYVGN 

       430        440        450        460        470        480 
EKASAETVDK EGWLKTGDLC YFDSEDFLYI VDRLKELIKY KAYQVPPVEL EQILHSNPDV 

       490        500        510        520        530        540 
IDAAVVPFPD EDAGEIPMAF IVRKPGSNLN EAQIIDFVAK QVTPYKKVRR VAFINAIPKN 

       550        560 
PAGKILRREL TKIAVDGNAS KL 

« Hide

References

« Hide 'large scale' references
[1]"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: 12805634] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION.
Strain: cv. Wassilewskija.
[2]"Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase genes."
Lawrence P.K.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[7]"The substrate specificity-determining amino acid code of 4-coumarate:CoA ligase."
Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D., Kombrink E., Stuible H.-P.
Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003) [PubMed: 12819348] [Abstract]
Cited for: GENE FAMILY ORGANIZATION.
[8]"A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid."
Schneider K., Kienow L., Schmelzer E., Colby T., Bartsch M., Miersch O., Wasternack C., Kombrink E., Stuible H.-P.
J. Biol. Chem. 280:13962-13972(2005) [PubMed: 15677481] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY250835 mRNA. Translation: AAP03018.1.
AY376731 mRNA. Translation: AAQ86590.1.
AB023035, AB007649 Genomic DNA. Translation: BAB10742.1.
CP002688 Genomic DNA. Translation: AED97741.1.
AY136459 mRNA. Translation: AAM97124.1.
BT010394 mRNA. Translation: AAQ56837.1.
IPIIPI00541683.
RefSeqNP_201143.1. NM_125733.2.
UniGeneAt.27966.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ84P23.
SMRQ84P23. Positions 23-553.
ModBaseSearch...

Proteomic databases

PRIDEQ84P23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G63380.1; AT5G63380.1; AT5G63380.
GeneID836457.
GenomeReviewsGene locus AT5G63380 in contig BA000015_GR.
KEGGath:AT5G63380.
NMPDRfig|3702.1.peg.28385.

Organism-specific databases

TAIRAt5g63380.

Phylogenomic databases

eggNOGKOG1176.
GeneTreeEPGT00070000028073.
HOGENOMHBG547964.
InParanoidQ84P23.
OMAGRISENM.
PhylomeDBQ84P23.
ProtClustDBCLSN2916910.

Gene expression databases

GenevestigatorQ84P23.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name4CLL9_ARATH
AccessionPrimary (citable) accession number: Q84P23
Secondary accession number(s): Q9FGW4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: September 21, 2011
This is version 48 of the entry and version 2 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