ACMAT_VITLA
ID ACMAT_VITLA Reviewed; 449 AA.
AC Q3ZPN4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Methanol O-anthraniloyltransferase;
DE EC=2.3.1.232;
DE AltName: Full=Anthraniloyl-CoA:methanol acyltransferase;
DE AltName: Full=Benzyl alcohol O-benzoyltransferase;
DE EC=2.3.1.196;
GN Name=AMAT;
OS Vitis labrusca (Concord grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=103355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=16262710; DOI=10.1111/j.1365-313x.2005.02552.x;
RA Wang J., De Luca V.;
RT "The biosynthesis and regulation of biosynthesis of Concord grape fruit
RT esters, including 'foxy' methylanthranilate.";
RL Plant J. 44:606-619(2005).
CC -!- FUNCTION: Acyltransferase that catalyzes the formation of methyl
CC anthranilate, a compound implicated in the 'foxy' odor character of
CC Concord grapes. Can use a variety of alcohol substrates when assayed
CC with both benzoyl-CoA and anthraniloyl-CoA.
CC {ECO:0000269|PubMed:16262710}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate;
CC Xref=Rhea:RHEA:37659, ChEBI:CHEBI:17790, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57331, ChEBI:CHEBI:73244; EC=2.3.1.232;
CC Evidence={ECO:0000269|PubMed:16262710};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + benzyl alcohol = benzyl benzoate + CoA;
CC Xref=Rhea:RHEA:30411, ChEBI:CHEBI:17987, ChEBI:CHEBI:41237,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57369; EC=2.3.1.196;
CC Evidence={ECO:0000269|PubMed:16262710};
CC -!- ACTIVITY REGULATION: K(+), Ca(2+), Mg(2+) and Mn(2+) increase enzyme
CC activity while Cu(2+) and Zn(2+) inactivate the enzyme.
CC {ECO:0000269|PubMed:16262710}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.8 uM for benzoyl-CoA (with native enzyme, in the presence of
CC benzyl alcohol) {ECO:0000269|PubMed:16262710};
CC KM=2.51 uM for anthraniloyl-CoA (with native enzyme, in the presence
CC of methanol) {ECO:0000269|PubMed:16262710};
CC KM=14.97 uM for methanol (with native enzyme, in the presence of
CC anthraniloyl-CoA) {ECO:0000269|PubMed:16262710};
CC KM=8.42 uM for benzoyl-CoA (with recombinant enzyme, in the presence
CC of benzyl alcohol) {ECO:0000269|PubMed:16262710};
CC KM=4.78 uM for anthraniloyl-CoA (with recombinant enzyme, in the
CC presence of methanol) {ECO:0000269|PubMed:16262710};
CC KM=31.8 uM for methanol (with recombinant enzyme, in the presence of
CC anthraniloyl-CoA) {ECO:0000269|PubMed:16262710};
CC Note=kcat is 0.045 sec(-1) with benzoyl-CoA as substrate (with native
CC enzyme). kcat is 0.022 sec(-1) with anthraniloyl-CoA as substrate
CC (with native enzyme). kcat is 0.0035 sec(-1) with methanol as
CC substrate (with native enzyme). kcat is 0.045 sec(-1) with benzoyl-
CC CoA as substrate (with recombinant enzyme). kcat is 0.01 sec(-1) with
CC anthraniloyl-CoA as substrate (with recombinant enzyme). kcat is
CC 0.0058 sec(-1) with methanol as substrate (with recombinant enzyme).;
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:16262710};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16262710}.
CC -!- TISSUE SPECIFICITY: Expressed in berry outer mesocarp, but not in berry
CC skin. {ECO:0000269|PubMed:16262710}.
CC -!- DEVELOPMENTAL STAGE: Expression starts when the berries began to change
CC the color. It increases throughout berry development to reach a maximum
CC level in very mature berries. {ECO:0000269|PubMed:16262710}.
CC -!- MISCELLANEOUS: No AMAT activity can be detected in Vitis vinifera
CC grapes. {ECO:0000305|PubMed:16262710}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY705388; AAW22989.1; -; mRNA.
DR AlphaFoldDB; Q3ZPN4; -.
DR SMR; Q3ZPN4; -.
DR KEGG; ag:AAW22989; -.
DR BRENDA; 2.3.1.196; 13227.
DR BRENDA; 2.3.1.232; 13227.
DR SABIO-RK; Q3ZPN4; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Transferase.
FT CHAIN 1..449
FT /note="Methanol O-anthraniloyltransferase"
FT /id="PRO_0000423915"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 50182 MW; 443AC243353D93F4 CRC64;
MASPSSPLVF SVNRCVPQIV RPANPTPREV KQLSDIDDQE GRRFQIPVIM FYRNNPLMEG
KDPVKVIREA LGKALVYYYP FAGRLIEGDN RKLMVDCTGE GVLFIEADAD TTLENLGDAI
QPMCPCFEEL LYDVPGSTTI LGSPLILIQV TRLRCGGFIF ALRLNHTMSD AAGLIQFLDT
IGEMAQGLSV PSLLPIWQRE LLNARNPPRI TRIHHEYEKV TNTKGTLMAM DENSLVHRSF
FFGREEIRAL RNRLPASLGA CSTFEVLMAC VWRCRTIAFA VDPDEVVRIS CIINMRGKHG
FELPPGYYGN AFVTPASITK AGMLCKNPLE FAIRLVKKAK AEMSQEYIKS VADLMVIKGR
PLFTQPGNFT VSDVTRAGLG EVDFGWGKPV YGGVARACPI ISFRMLFRNS KGEEGSVIPI
WLPPPVMERF EQELKRMTKK AELLITSML
