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

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Ref.5

Subcellular location

Peroxisome. Ref.5

Induction

By methyl jasmonate. Ref.5

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

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Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
Oxylipin biosynthesis
   Cellular componentPeroxisome
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processjasmonic acid biosynthetic process Ref.5

Inferred from direct assay. Source: TAIR

   Cellular componentperoxisome Ref.5

Inferred from direct assay. Source: TAIR

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fatty-acyl-CoA synthase activity Ref.5

Inferred from direct assay. Source: TAIR

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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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

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Sequences

Sequence LengthMass (Da)Tools
Q9M0X9-1 [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

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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]"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.
[4]"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.
[5]"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.

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Cross-references

Sequence databases

AY250839 mRNA. Translation: AAP03022.1.
AL161502 Genomic DNA. Translation: CAB81058.1.
AY091079 mRNA. Translation: AAM13899.1.
AY122950 mRNA. Translation: AAM67483.1.
IPIIPI00536809.
PIRH85064.
RefSeqNP_192425.1.
UniGeneAt.33913

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBaseSearch...

Proteomic databases

PRIDEQ9M0X9.
ProMEXQ9M0X9.

Genome annotation databases

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

Organism-specific databases

TAIRAt4g05160.

Phylogenomic databases

OMAQ9M0X9. QIVSVET.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents