CHAT_ARATH
ID CHAT_ARATH Reviewed; 454 AA.
AC Q9SRQ2; Q8LFV6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=(Z)-3-hexen-1-ol acetyltransferase;
DE EC=2.3.1.195;
GN Name=CHAT; OrderedLocusNames=At3g03480; ORFNames=T21P5.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12226525; DOI=10.1104/pp.006460;
RA D'Auria J.C., Chen F., Pichersky E.;
RT "Characterization of an acyltransferase capable of synthesizing
RT benzylbenzoate and other volatile esters in flowers and damaged leaves of
RT Clarkia breweri.";
RL Plant Physiol. 130:466-476(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TISSUE SPECIFICITY,
RP INDUCTION BY WOUNDING, AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17163881; DOI=10.1111/j.1365-313x.2006.02946.x;
RA D'Auria J.C., Pichersky E., Schaub A., Hansel A., Gershenzon J.;
RT "Characterization of a BAHD acyltransferase responsible for producing the
RT green leaf volatile (Z)-3-hexen-1-yl acetate in Arabidopsis thaliana.";
RL Plant J. 49:194-207(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acyltransferase involved in the production of green leaf
CC volatiles (GLVs). Uses acetyl-CoA as substrate, but not malonyl-CoA or
CC benzoyl-CoA. Prefers primary, medium-chain-length, aliphatic alcohols.
CC {ECO:0000269|PubMed:17163881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-hex-3-en-1-ol + acetyl-CoA = (3Z)-hex-3-en-1-yl acetate +
CC CoA; Xref=Rhea:RHEA:28254, ChEBI:CHEBI:28857, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61316; EC=2.3.1.195;
CC Evidence={ECO:0000269|PubMed:12226525, ECO:0000269|PubMed:17163881};
CC -!- ACTIVITY REGULATION: Inhibited by magnesium, calcium, cobalt, zinc and
CC copper. {ECO:0000269|PubMed:17163881}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.5 uM for acetyl-CoA {ECO:0000269|PubMed:12226525,
CC ECO:0000269|PubMed:17163881};
CC KM=165 uM for (3Z)-hex-3-en-ol {ECO:0000269|PubMed:12226525,
CC ECO:0000269|PubMed:17163881};
CC KM=174 uM for 1-octanol {ECO:0000269|PubMed:12226525,
CC ECO:0000269|PubMed:17163881};
CC pH dependence:
CC Optimum pH is 7.1-7.3. {ECO:0000269|PubMed:12226525,
CC ECO:0000269|PubMed:17163881};
CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems. Lower levels in
CC flowers and barely detected in roots and siliques.
CC {ECO:0000269|PubMed:17163881}.
CC -!- INDUCTION: Up-regulated by wounding with a peak 3 hours after wounding.
CC {ECO:0000269|PubMed:17163881}.
CC -!- DISRUPTION PHENOTYPE: Loss of (3Z)-hex-3-en-1-yl acetate production.
CC {ECO:0000269|PubMed:17163881}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AF500201; AAN09797.1; -; mRNA.
DR EMBL; AC009895; AAF01587.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73949.1; -; Genomic_DNA.
DR EMBL; AY084623; AAM61186.1; -; mRNA.
DR RefSeq; NP_186998.1; NM_111219.3.
DR AlphaFoldDB; Q9SRQ2; -.
DR SMR; Q9SRQ2; -.
DR STRING; 3702.AT3G03480.1; -.
DR PaxDb; Q9SRQ2; -.
DR PRIDE; Q9SRQ2; -.
DR ProteomicsDB; 222076; -.
DR EnsemblPlants; AT3G03480.1; AT3G03480.1; AT3G03480.
DR GeneID; 821249; -.
DR Gramene; AT3G03480.1; AT3G03480.1; AT3G03480.
DR KEGG; ath:AT3G03480; -.
DR Araport; AT3G03480; -.
DR TAIR; locus:2099704; AT3G03480.
DR eggNOG; ENOG502QV0F; Eukaryota.
DR HOGENOM; CLU_014546_2_2_1; -.
DR InParanoid; Q9SRQ2; -.
DR OMA; MPPVWER; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9SRQ2; -.
DR BioCyc; ARA:AT3G03480-MON; -.
DR BioCyc; MetaCyc:AT3G03480-MON; -.
DR BRENDA; 2.3.1.195; 399.
DR SABIO-RK; Q9SRQ2; -.
DR PRO; PR:Q9SRQ2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRQ2; baseline and differential.
DR Genevisible; Q9SRQ2; AT.
DR GO; GO:0102165; F:(Z)-3-hexen-1-ol acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010327; F:acetyl CoA:(Z)-3-hexen-1-ol acetyltransferase activity; IDA:TAIR.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; TAS:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="(Z)-3-hexen-1-ol acetyltransferase"
FT /id="PRO_0000409589"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CONFLICT 338
FT /note="A -> V (in Ref. 5; AAM61186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50290 MW; C684495199FCCFB2 CRC64;
MDHQVSLPQS TTTGLSFKVH RQQRELVTPA KPTPRELKPL SDIDDQQGLR FQIPVIFFYR
PNLSSDLDPV QVIKKALADA LVYYYPFAGR LRELSNRKLA VDCTGEGVLF IEAEADVALA
ELEEADALLP PFPFLEELLF DVEGSSDVLN TPLLLVQVTR LKCCGFIFAL RFNHTMTDGA
GLSLFLKSLC ELACGLHAPS VPPVWNRHLL TVSASEARVT HTHREYDDQV GIDVVATGHP
LVSRSFFFRA EEISAIRKLL PPDLHNTSFE ALSSFLWRCR TIALNPDPNT EMRLTCIINS
RSKLRNPPLE PGYYGNVFVI PAAIATARDL IEKPLEFALR LIQETKSSVT EDYVRSVTAL
MATRGRPMFV ASGNYIISDL RHFDLGKIDF GPWGKPVYGG TAKAGIALFP GVSFYVPFKN
KKGETGTVVA ISLPVRAMET FVAELNGVLN VSKG
