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Q9M0X9 (4CLL7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. 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
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 7
EC=6.2.1.-
Alternative name(s):
4-coumarate--CoA ligase isoform 6
Short name=At4CL6
Gene names
Name:4CLL7
Ordered Locus Names:At4g05160
ORF Names:C17L7.80
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length544 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. Ref.6

Subcellular location

Peroxisome Ref.6.

Induction

By methyl jasmonate. Ref.6

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=9 µM for nonanoic acid

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.6. Source: TAIR

   Cellular componentperoxisome

Inferred from direct assay Ref.6. Source: TAIR

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fatty-acyl-CoA synthase activity

Inferred from direct assay Ref.6. 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 – 5445444-coumarate--CoA ligase-like 7
PRO_0000299180

Regions

Nucleotide binding198 – 2069ATP By similarity
Nucleotide binding339 – 3446ATP By similarity
Region269 – 33870SBD1 By similarity
Region339 – 40365SBD2 By similarity
Motif542 – 5443Microbody targeting signal Potential

Sites

Binding site4241ATP By similarity
Binding site4391ATP By similarity
Binding site5301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9M0X9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B2422848E70D2909

FASTA54459,850
        10         20         30         40         50         60 
MEKSGYGRDG IYRSLRPTLV LPKDPNTSLV SFLFRNSSSY PSKLAIADSD TGDSLTFSQL 

        70         80         90        100        110        120 
KSAVARLAHG FHRLGIRKND VVLIFAPNSY QFPLCFLAVT AIGGVFTTAN PLYTVNEVSK 

       130        140        150        160        170        180 
QIKDSNPKII ISVNQLFDKI KGFDLPVVLL GSKDTVEIPP GSNSKILSFD NVMELSEPVS 

       190        200        210        220        230        240 
EYPFVEIKQS DTAALLYSSG TTGTSKGVEL THGNFIAASL MVTMDQDLMG EYHGVFLCFL 

       250        260        270        280        290        300 
PMFHVFGLAV ITYSQLQRGN ALVSMARFEL ELVLKNIEKF RVTHLWVVPP VFLALSKQSI 

       310        320        330        340        350        360 
VKKFDLSSLK YIGSGAAPLG KDLMEECGRN IPNVLLMQGY GMTETCGIVS VEDPRLGKRN 

       370        380        390        400        410        420 
SGSAGMLAPG VEAQIVSVET GKSQPPNQQG EIWVRGPNMM KGYLNNPQAT KETIDKKSWV 

       430        440        450        460        470        480 
HTGDLGYFNE DGNLYVVDRI KELIKYKGFQ VAPAELEGLL VSHPDILDAV VIPFPDEEAG 

       490        500        510        520        530        540 
EVPIAFVVRS PNSSITEQDI QKFIAKQVAP YKRLRRVSFI SLVPKSAAGK ILRRELVQQV 


RSKM

« 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]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
[5]"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.
[6]"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, ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY250839 mRNA. Translation: AAP03022.1.
AL161502 Genomic DNA. Translation: CAB81058.1.
CP002687 Genomic DNA. Translation: AEE82486.1.
AY091079 mRNA. Translation: AAM13899.1.
AY122950 mRNA. Translation: AAM67483.1.
IPIIPI00536809.
PIRH85064.
RefSeqNP_192425.1. NM_116755.4.
UniGeneAt.33913.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ9M0X9.
SMRQ9M0X9. Positions 10-539.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9M0X9.

Proteomic databases

PRIDEQ9M0X9.
ProMEXQ9M0X9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G05160.1; AT4G05160.1; AT4G05160.
GeneID825864.
GenomeReviewsGene locus AT4G05160 in contig CT486007_GR.
KEGGath:AT4G05160.
NMPDRfig|3702.1.peg.18335.

Organism-specific databases

TAIRAt4g05160.

Phylogenomic databases

eggNOGKOG1176.
GeneTreeEPGT00070000028073.
HOGENOMHBG547964.
InParanoidQ9M0X9.
OMAYRSLRPT.
PhylomeDBQ9M0X9.
ProtClustDBCLSN2685605.

Gene expression databases

GenevestigatorQ9M0X9.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01904.
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name4CLL7_ARATH
AccessionPrimary (citable) accession number: Q9M0X9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 64 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents