HST_TOBAC
ID HST_TOBAC Reviewed; 435 AA.
AC Q8GSM7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Shikimate O-hydroxycinnamoyltransferase;
DE EC=2.3.1.133;
DE AltName: Full=Hydroxycinnamoyl transferase;
DE AltName: Full=Hydroxycinnamoyl-Coenzyme A shikimate/quinate hydroxycinnamoyltransferase;
GN Name=HST; Synonyms=HCT;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Stem;
RX PubMed=12381722; DOI=10.1074/jbc.m209362200;
RA Hoffmann L., Maury S., Martz F., Geoffroy P., Legrand M.;
RT "Purification, cloning, and properties of an acyltransferase controlling
RT shikimate and quinate ester intermediates in phenylpropanoid metabolism.";
RL J. Biol. Chem. 278:95-103(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=15161961; DOI=10.1105/tpc.020297;
RA Hoffmann L., Besseau S., Geoffroy P., Ritzenthaler C., Meyer D.,
RA Lapierre C., Pollet B., Legrand M.;
RT "Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate
RT hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis.";
RL Plant Cell 16:1446-1465(2004).
CC -!- FUNCTION: Acyltransferase involved in the biosynthesis of lignin. The
CC affinity for shikimate as acceptor is 100-fold higher than for quinate.
CC The most efficient donors are caffeoyl-CoA > p-coumaroyl-CoA >
CC feruloyl-CoA >> sinapoyl-CoA. {ECO:0000269|PubMed:12381722,
CC ECO:0000269|PubMed:15161961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-coumaroyl-CoA + shikimate = CoA + trans-4-
CC coumaroylshikimate; Xref=Rhea:RHEA:12124, ChEBI:CHEBI:36208,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57768;
CC EC=2.3.1.133; Evidence={ECO:0000269|PubMed:12381722,
CC ECO:0000269|PubMed:15161961};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=600 uM for p-coumaroyl-CoA (with shikimate as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC KM=50 uM for caffeoyl-CoA (with shikimate as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC KM=350 uM for feruloyl-CoA (with shikimate as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC KM=150 uM for p-coumaroyl-CoA (with quinate as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC KM=730 uM for caffeoyl-CoA (with quinate as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC KM=750 uM for shikimate (with p-coumaroyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC KM=70.1 uM for quinate (with p-coumaroyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:12381722};
CC Vmax=65 pmol/sec/mg enzyme with p-coumaroyl-CoA as substrate and
CC shikimate as cosubstrate {ECO:0000269|PubMed:12381722};
CC Vmax=15 pmol/sec/mg enzyme with caffeoyl-CoA as substrate and
CC shikimate as cosubstrate {ECO:0000269|PubMed:12381722};
CC Vmax=10 pmol/sec/mg enzyme with feruloyl-CoA as substrate and
CC shikimate as cosubstrate {ECO:0000269|PubMed:12381722};
CC Vmax=4.6 pmol/sec/mg enzyme with p-coumaroyl-CoA as substrate and
CC quinate as cosubstrate {ECO:0000269|PubMed:12381722};
CC Vmax=1.4 pmol/sec/mg enzyme with caffeoyl-CoA as substrate and
CC quinate as cosubstrate {ECO:0000269|PubMed:12381722};
CC Vmax=140 pmol/sec/mg enzyme with shikimate as substrate and p-
CC coumaroyl-CoA as cosubstrate {ECO:0000269|PubMed:12381722};
CC Vmax=21 pmol/sec/mg enzyme with quinate as substrate and p-coumaroyl-
CC CoA as cosubstrate {ECO:0000269|PubMed:12381722};
CC -!- TISSUE SPECIFICITY: Highly expressed in stem vascular tissues.
CC {ECO:0000269|PubMed:15161961}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AJ507825; CAD47830.1; -; mRNA.
DR RefSeq; NP_001312552.1; NM_001325623.1.
DR RefSeq; XP_016474935.1; XM_016619449.1.
DR AlphaFoldDB; Q8GSM7; -.
DR SMR; Q8GSM7; -.
DR STRING; 4097.Q8GSM7; -.
DR GeneID; 107796658; -.
DR KEGG; nta:107796658; -.
DR OMA; LWNSGPD; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q8GSM7; -.
DR BioCyc; MetaCyc:MON-12138; -.
DR BRENDA; 2.3.1.133; 3645.
DR BRENDA; 2.3.1.99; 3645.
DR SABIO-RK; Q8GSM7; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0047172; F:shikimate O-hydroxycinnamoyltransferase activity; IEA:UniProtKB-EC.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..435
FT /note="Shikimate O-hydroxycinnamoyltransferase"
FT /id="PRO_0000409593"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="A -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48265 MW; A4808B12FC6C5A0A CRC64;
MKIEVKESTM VKPAAETPQQ RLWNSNVDLV VPNFHTPSVY FYRPTGSPNF FDGKVLKEAL
SKALVPFYPM AGRLCRDEDG RIEIDCKGQG VLFVEAESDG VVDDFGDFAP TLELRQLIPA
VDYSQGIQSY ALLVLQITHF KCGGVSLGVG MQHHAADGAS GLHFINTWSD MARGLDLTIP
PFIDRTLLRA RDPPQPQFPH VEYQPPPTLK VTPENTPISE AVPETSVSIF KLTRDQINTL
KAKSKEDGNT VNYSSYEMLA GHVWRSTCMA RGLAHDQETK LYIATDGRSR LRPSLPPGYF
GNVIFTTTPI AVAGDIQSKP IWYAASKLHD ALARMDNDYL RSALDYLELQ PDLKALVRGA
HTFKCPNLGI TSWSRLPIHD ADFGWGRPIF MGPGGIAYEG LSFILPSPTN DGSQSVAISL
QAEHMKLFEK FLYDF
