HST_ARATH
ID HST_ARATH Reviewed; 433 AA.
AC Q9FI78; Q8LFT5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Shikimate O-hydroxycinnamoyltransferase {ECO:0000303|PubMed:15161961};
DE EC=2.3.1.133 {ECO:0000269|PubMed:15161961, ECO:0000269|PubMed:27805809};
DE AltName: Full=Hydroxycinnamoyl transferase {ECO:0000303|PubMed:15161961, ECO:0000303|PubMed:26858288};
DE Short=AtHCT {ECO:0000303|PubMed:26858288};
DE AltName: Full=Hydroxycinnamoyl-Coenzyme A shikimate/quinate hydroxycinnamoyltransferase {ECO:0000303|PubMed:15161961};
GN Name=HST;
GN Synonyms=HCT {ECO:0000303|PubMed:15161961, ECO:0000303|PubMed:26858288,
GN ECO:0000303|PubMed:27805809};
GN OrderedLocusNames=At5g48930 {ECO:0000312|Araport:AT5G48930};
GN ORFNames=K19E20.4 {ECO:0000312|EMBL:BAB10316.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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.
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=26858288; DOI=10.1093/pcp/pcw016;
RA Eudes A., Pereira J.H., Yogiswara S., Wang G., Teixeira Benites V.,
RA Baidoo E.E.K., Lee T.S., Adams P.D., Keasling J.D., Loque D.;
RT "Exploiting the substrate promiscuity of hydroxycinnamoyl-CoA:shikimate
RT hydroxycinnamoyl transferase to reduce lignin.";
RL Plant Cell Physiol. 57:568-579(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH 4-COUMAROYL-COA,
RP ACTIVE SITES, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27805809; DOI=10.1021/acs.biochem.6b00887;
RA Levsh O., Chiang Y.-C., Tung C.F., Noel J.P., Wang Y., Weng J.-K.;
RT "Dynamic conformational states dictate selectivity toward the native
RT substrate in a substrate-permissive acyltransferase.";
RL Biochemistry 55:6314-6326(2016).
CC -!- FUNCTION: Acyltransferase involved in the biosynthesis of lignin
CC (PubMed:15161961, PubMed:26858288, PubMed:27805809). Accepts caffeoyl-
CC CoA and p-coumaroyl-CoA as substrates and transfers the acyl group on
CC both shikimate and quinate acceptors (PubMed:15161961).
CC {ECO:0000269|PubMed:15161961, ECO:0000269|PubMed:26858288,
CC ECO:0000269|PubMed:27805809}.
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:15161961,
CC ECO:0000269|PubMed:27805809};
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AB017061; BAB10316.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95744.1; -; Genomic_DNA.
DR EMBL; BT026488; ABH04595.1; -; mRNA.
DR EMBL; AK226213; BAE98378.1; -; mRNA.
DR EMBL; AY084652; AAM61215.1; -; mRNA.
DR RefSeq; NP_199704.1; NM_124270.4.
DR PDB; 5KJS; X-ray; 2.20 A; A=1-433.
DR PDB; 5KJT; X-ray; 2.50 A; A=1-433.
DR PDB; 5KJU; X-ray; 2.44 A; A=1-433.
DR PDBsum; 5KJS; -.
DR PDBsum; 5KJT; -.
DR PDBsum; 5KJU; -.
DR AlphaFoldDB; Q9FI78; -.
DR SMR; Q9FI78; -.
DR BioGRID; 20197; 4.
DR IntAct; Q9FI78; 2.
DR STRING; 3702.AT5G48930.1; -.
DR PaxDb; Q9FI78; -.
DR PRIDE; Q9FI78; -.
DR ProteomicsDB; 232138; -.
DR DNASU; 834951; -.
DR EnsemblPlants; AT5G48930.1; AT5G48930.1; AT5G48930.
DR GeneID; 834951; -.
DR Gramene; AT5G48930.1; AT5G48930.1; AT5G48930.
DR KEGG; ath:AT5G48930; -.
DR Araport; AT5G48930; -.
DR TAIR; locus:2154334; AT5G48930.
DR eggNOG; ENOG502QTJX; Eukaryota.
DR HOGENOM; CLU_014546_2_0_1; -.
DR InParanoid; Q9FI78; -.
DR OMA; AIQHTRF; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9FI78; -.
DR BioCyc; ARA:AT5G48930-MON; -.
DR BRENDA; 2.3.1.133; 399.
DR PRO; PR:Q9FI78; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI78; baseline and differential.
DR Genevisible; Q9FI78; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0047205; F:quinate O-hydroxycinnamoyltransferase activity; IMP:TAIR.
DR GO; GO:0047172; F:shikimate O-hydroxycinnamoyltransferase activity; IMP:TAIR.
DR GO; GO:0010252; P:auxin homeostasis; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IMP:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell wall biogenesis/degradation;
KW Reference proteome; Transferase.
FT CHAIN 1..433
FT /note="Shikimate O-hydroxycinnamoyltransferase"
FT /id="PRO_0000409592"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27805809"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27805809"
FT BINDING 252..255
FT /ligand="4-coumaroyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57355"
FT /evidence="ECO:0000269|PubMed:27805809,
FT ECO:0007744|PDB:5KJT"
FT BINDING 284..290
FT /ligand="4-coumaroyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57355"
FT /evidence="ECO:0000269|PubMed:27805809,
FT ECO:0007744|PDB:5KJT"
FT BINDING 370..373
FT /ligand="4-coumaroyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57355"
FT /evidence="ECO:0000269|PubMed:27805809,
FT ECO:0007744|PDB:5KJT"
FT CONFLICT 125
FT /note="A -> T (in Ref. 5; AAM61215)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:5KJS"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:5KJS"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:5KJS"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5KJT"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:5KJS"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5KJU"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:5KJU"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 253..268
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:5KJS"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 335..347
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:5KJU"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:5KJS"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 420..425
FT /evidence="ECO:0007829|PDB:5KJS"
FT HELIX 426..430
FT /evidence="ECO:0007829|PDB:5KJS"
SQ SEQUENCE 433 AA; 47975 MW; 044EB211DAFA45AC CRC64;
MKINIRDSTM VRPATETPIT NLWNSNVDLV IPRFHTPSVY FYRPTGASNF FDPQVMKEAL
SKALVPFYPM AGRLKRDDDG RIEIDCNGAG VLFVVADTPS VIDDFGDFAP TLNLRQLIPE
VDHSAGIHSF PLLVLQVTFF KCGGASLGVG MQHHAADGFS GLHFINTWSD MARGLDLTIP
PFIDRTLLRA RDPPQPAFHH VEYQPAPSMK IPLDPSKSGP ENTTVSIFKL TRDQLVALKA
KSKEDGNTVS YSSYEMLAGH VWRSVGKARG LPNDQETKLY IATDGRSRLR PQLPPGYFGN
VIFTATPLAV AGDLLSKPTW YAAGQIHDFL VRMDDNYLRS ALDYLEMQPD LSALVRGAHT
YKCPNLGITS WVRLPIYDAD FGWGRPIFMG PGGIPYEGLS FVLPSPTNDG SLSVAIALQS
EHMKLFEKFL FEI
