HHT1_ARATH
ID HHT1_ARATH Reviewed; 457 AA.
AC Q94CD1; Q9FLM5;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Omega-hydroxypalmitate O-feruloyl transferase;
DE EC=2.3.1.188;
DE AltName: Full=Omega-hydroxyacid hydroxycinnamoyltransferase;
DE AltName: Full=Protein ALIPHATIC SUBERIN FERULOYL TRANSFERASE;
GN Name=HHT1; Synonyms=ASFT; OrderedLocusNames=At5g41040; ORFNames=MEE6.11;
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], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19846769; DOI=10.1073/pnas.0905555106;
RA Gou J.Y., Yu X.H., Liu C.J.;
RT "A hydroxycinnamoyltransferase responsible for synthesizing suberin
RT aromatics in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18855-18860(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19759341; DOI=10.1104/pp.109.144907;
RA Molina I., Li-Beisson Y., Beisson F., Ohlrogge J.B., Pollard M.;
RT "Identification of an Arabidopsis feruloyl-coenzyme A transferase required
RT for suberin synthesis.";
RL Plant Physiol. 151:1317-1328(2009).
CC -!- FUNCTION: Involved in the synthesis of aromatics of the suberin
CC polymer. Specifically affects the accumulation of the ferulate
CC constituent of suberin in roots and seeds, but has no effect on the
CC content of p-coumarate or sinapate. {ECO:0000269|PubMed:19759341,
CC ECO:0000269|PubMed:19846769}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-feruloyl-CoA + 16-hydroxyhexadecanoate = 16-
CC feruloyloxyhexadecanoate + CoA; Xref=Rhea:RHEA:26470,
CC ChEBI:CHEBI:55329, ChEBI:CHEBI:55331, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:87305; EC=2.3.1.188;
CC Evidence={ECO:0000269|PubMed:19759341, ECO:0000269|PubMed:19846769};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.7 uM for feruloyl-CoA;
CC KM=36.7 uM for p-coumaroyl-CoA;
CC KM=5.1 uM for 16-OH-palmitic acid;
CC Note=16-hydroxypalmitic acid is the main acyl acceptor.;
CC pH dependence:
CC Optimum pH is 7.5.;
CC Temperature dependence:
CC Optimum temperature is 10 degrees Celsius.;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94CD1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves, stems,
CC flowers and siliques. Detected at the protein level in roots and in
CC seed coats. {ECO:0000269|PubMed:19759341, ECO:0000269|PubMed:19846769}.
CC -!- DEVELOPMENTAL STAGE: Detected in seed coats in the inner layer of the
CC outer integument at the beginning of the desiccation stage. Also
CC expressed at the chalazal region as desiccation proceeds.
CC -!- DISRUPTION PHENOTYPE: Elimination of suberin-associated ester-linked
CC ferulate. Altered permeability and sensitivity of seeds and roots to
CC salt stress. {ECO:0000269|PubMed:19759341,
CC ECO:0000269|PubMed:19846769}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09706.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ176867; ACY78659.1; -; mRNA.
DR EMBL; AB010072; BAB09706.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94628.1; -; Genomic_DNA.
DR EMBL; AY034954; AAK59460.1; -; mRNA.
DR EMBL; AY062996; AAL34170.1; -; mRNA.
DR RefSeq; NP_568587.2; NM_123469.2.
DR RefSeq; NP_851111.1; NM_180780.2. [Q94CD1-1]
DR AlphaFoldDB; Q94CD1; -.
DR SMR; Q94CD1; -.
DR STRING; 3702.AT5G41040.1; -.
DR PaxDb; Q94CD1; -.
DR PRIDE; Q94CD1; -.
DR ProteomicsDB; 230224; -. [Q94CD1-1]
DR EnsemblPlants; AT5G41040.1; AT5G41040.1; AT5G41040. [Q94CD1-1]
DR GeneID; 834106; -.
DR Gramene; AT5G41040.1; AT5G41040.1; AT5G41040. [Q94CD1-1]
DR KEGG; ath:AT5G41040; -.
DR Araport; AT5G41040; -.
DR TAIR; locus:2162976; AT5G41040.
DR eggNOG; ENOG502QS3E; Eukaryota.
DR InParanoid; Q94CD1; -.
DR PhylomeDB; Q94CD1; -.
DR BioCyc; ARA:AT5G41040-MON; -.
DR PRO; PR:Q94CD1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94CD1; baseline and differential.
DR Genevisible; Q94CD1; AT.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0050734; F:hydroxycinnamoyltransferase activity; IDA:TAIR.
DR GO; GO:0102406; F:omega-hydroxypalmitate O-sinapoyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052325; P:cell wall pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0010345; P:suberin 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 Acyltransferase; Alternative splicing; Cell wall biogenesis/degradation;
KW Reference proteome; Transferase.
FT CHAIN 1..457
FT /note="Omega-hydroxypalmitate O-feruloyl transferase"
FT /id="PRO_0000392057"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
SQ SEQUENCE 457 AA; 50958 MW; 44AE9D12FB15A747 CRC64;
MVAENNKNKD VTLSASMDNN NNNIKGTNIH LEVHQKEPAL VKPESETRKG LYFLSNLDQN
IAVIVRTIYC FKSEERGNEE AVQVIKKALS QVLVHYYPLA GRLTISPEGK LTVDCTEEGV
VFVEAEANCK MDEIGDITKP DPETLGKLVY DVVDAKNILE IPPVTAQVTK FKCGGFVLGL
CMNHCMFDGI GAMEFVNSWG QVARGLPLTT PPFSDRTILN ARNPPKIENL HQEFEEIEDK
SNINSLYTKE PTLYRSFCFD PEKIKKLKLQ ATENSESLLG NSCTSFEALS AFVWRARTKS
LKMLSDQKTK LLFAVDGRAK FEPQLPKGYF GNGIVLTNSI CEAGELIEKP LSFAVGLVRE
AIKMVTDGYM RSAIDYFEVT RARPSLSSTL LITTWSRLGF HTTDFGWGEP ILSGPVALPE
KEVTLFLSHG EQRRSINVLL GLPATAMDVF QEQFLQI
