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Q9SRQ2 (CHAT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
(Z)-3-hexen-1-ol acetyltransferase

EC=2.3.1.195
Gene names
Name:CHAT
Ordered Locus Names:At3g03480
ORF Names:T21P5.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acyltransferase involved in the production of green leaf volatiles. Uses acetyl-CoA as substrate, but not malonyl-CoA or benzoyl-CoA. Prefers primary, medium-chain-length, aliphatic alcohols. Ref.2

Catalytic activity

Acetyl-CoA + (3Z)-hex-3-en-ol = (3Z)-hex-3-en-1-yl acetate + CoA. Ref.1 Ref.2

Enzyme regulation

Inhibited by magnesium, calcium, cobalt, zinc and copper. Ref.2

Tissue specificity

Expressed in leaves and stems. Lower levels in flowers and barely detected in roots and siliques. Ref.2

Induction

Up-regulated by wounding with a peak 3 hours after wounding. Ref.2

Disruption phenotype

Loss of (3Z)-hex-3-en-1-yl acetate production. Ref.2

Sequence similarities

Belongs to the plant acetyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=10.5 µM for acetyl CoA Ref.1 Ref.2

KM=165 µM for (3Z)-hex-3-en-ol

KM=174 µM for 1-octanol

pH dependence:

Optimum pH is 7.1-7.3.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454(Z)-3-hexen-1-ol acetyltransferase
PRO_0000409589

Experimental info

Sequence conflict3381A → V in AAM61186. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9SRQ2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C684495199FCCFB2

FASTA45450,290
        10         20         30         40         50         60 
MDHQVSLPQS TTTGLSFKVH RQQRELVTPA KPTPRELKPL SDIDDQQGLR FQIPVIFFYR 

        70         80         90        100        110        120 
PNLSSDLDPV QVIKKALADA LVYYYPFAGR LRELSNRKLA VDCTGEGVLF IEAEADVALA 

       130        140        150        160        170        180 
ELEEADALLP PFPFLEELLF DVEGSSDVLN TPLLLVQVTR LKCCGFIFAL RFNHTMTDGA 

       190        200        210        220        230        240 
GLSLFLKSLC ELACGLHAPS VPPVWNRHLL TVSASEARVT HTHREYDDQV GIDVVATGHP 

       250        260        270        280        290        300 
LVSRSFFFRA EEISAIRKLL PPDLHNTSFE ALSSFLWRCR TIALNPDPNT EMRLTCIINS 

       310        320        330        340        350        360 
RSKLRNPPLE PGYYGNVFVI PAAIATARDL IEKPLEFALR LIQETKSSVT EDYVRSVTAL 

       370        380        390        400        410        420 
MATRGRPMFV ASGNYIISDL RHFDLGKIDF GPWGKPVYGG TAKAGIALFP GVSFYVPFKN 

       430        440        450 
KKGETGTVVA ISLPVRAMET FVAELNGVLN VSKG 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of an acyltransferase capable of synthesizing benzylbenzoate and other volatile esters in flowers and damaged leaves of Clarkia breweri."
D'Auria J.C., Chen F., Pichersky E.
Plant Physiol. 130:466-476(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Characterization of a BAHD acyltransferase responsible for producing the green leaf volatile (Z)-3-hexen-1-yl acetate in Arabidopsis thaliana."
D'Auria J.C., Pichersky E., Schaub A., Hansel A., Gershenzon J.
Plant J. 49:194-207(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION BY WOUNDING, FUNCTION.
Strain: cv. Landsberg erecta.
[3]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF500201 mRNA. Translation: AAN09797.1.
AC009895 Genomic DNA. Translation: AAF01587.1.
CP002686 Genomic DNA. Translation: AEE73949.1.
AY084623 mRNA. Translation: AAM61186.1.
IPIIPI00537056.
RefSeqNP_186998.1. NM_111219.2.
UniGeneAt.40974.

3D structure databases

ProteinModelPortalQ9SRQ2.
SMRQ9SRQ2. Positions 18-441.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT3G03480.1-P.

Proteomic databases

PRIDEQ9SRQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID821249.
KEGGath:AT3G03480.

Organism-specific databases

TAIRAt3g03480.

Phylogenomic databases

eggNOGNOG323053.
HOGENOMHOG000237410.
InParanoidQ9SRQ2.
OMAIPVIQFY.
PhylomeDBQ9SRQ2.
ProtClustDBCLSN2684090.

Enzyme and pathway databases

BioCycMetaCyc:AT3G03480-MONOMER.

Gene expression databases

GenevestigatorQ9SRQ2.

Family and domain databases

Gene3D3.30.559.10. 2 hits.
InterProIPR023213. CAT-like_dom.
IPR003480. Transferase.
[Graphical view]
PfamPF02458. Transferase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHAT_ARATH
AccessionPrimary (citable) accession number: Q9SRQ2
Secondary accession number(s): Q8LFV6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 65 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