AHT1_ORYSJ
ID AHT1_ORYSJ Reviewed; 449 AA.
AC Q7XPK7; A3AYC9; Q0J9A2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Agmatine hydroxycinnamoyltransferase 1 {ECO:0000303|PubMed:27354554};
DE Short=OsAHT1 {ECO:0000303|PubMed:27354554};
DE EC=2.3.1.- {ECO:0000305};
DE AltName: Full=Agmatine hydroxycinnamoyl transferase {ECO:0000303|PubMed:24908251};
GN Name=AHT1 {ECO:0000303|PubMed:27354554};
GN OrderedLocusNames=Os04g0664600 {ECO:0000312|EMBL:BAS91492.1},
GN LOC_Os04g56910 {ECO:0000305};
GN ORFNames=OsJ_16526 {ECO:0000312|EMBL:EAZ32318.1},
GN OSJNBa0087O24.2 {ECO:0000312|EMBL:CAE03579.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION.
RX PubMed=24908251; DOI=10.1038/ng.3007;
RA Chen W., Gao Y., Xie W., Gong L., Lu K., Wang W., Li Y., Liu X., Zhang H.,
RA Dong H., Zhang W., Zhang L., Yu S., Wang G., Lian X., Luo J.;
RT "Genome-wide association analyses provide genetic and biochemical insights
RT into natural variation in rice metabolism.";
RL Nat. Genet. 46:714-721(2014).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=27015846; DOI=10.1111/jipb.12480;
RA Tanabe K., Hojo Y., Shinya T., Galis I.;
RT "Molecular evidence for biochemical diversification of phenolamide
RT biosynthesis in rice plants.";
RL J. Integr. Plant Biol. 58:903-913(2016).
RN [8]
RP FUNCTION.
RX PubMed=27354554; DOI=10.1105/tpc.16.00265;
RA Peng M., Gao Y., Chen W., Wang W., Shen S., Shi J., Wang C., Zhang Y.,
RA Zou L., Wang S., Wan J., Liu X., Gong L., Luo J.;
RT "Evolutionarily distinct BAHD N-acyltransferases are responsible for
RT natural variation of aromatic amine conjugates in rice.";
RL Plant Cell 28:1533-1550(2016).
CC -!- FUNCTION: Hydroxycinnamoyl transferase that catalyzes the transfer of
CC an acyl from p-coumaryol-CoA to agmatine, to produce coumaroyl
CC agmatine. Can use feruloyl-CoA, caffeoyl-CoA and sinapoyl-CoA as acyl
CC donors (PubMed:24908251, PubMed:27015846, PubMed:27354554). Seems to be
CC able to transfer the acyl group from p-coumaroyl-CoA and feruloyl-CoA
CC to the acyl acceptors putrescine and spermidine (PubMed:24908251).
CC {ECO:0000269|PubMed:24908251, ECO:0000269|PubMed:27015846,
CC ECO:0000269|PubMed:27354554}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=43.6 uM for feruloyl-CoA {ECO:0000269|PubMed:27015846};
CC KM=45.3 uM for agmatine {ECO:0000269|PubMed:27015846};
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed at low levels
CC in flowers. {ECO:0000269|PubMed:27015846}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AL606646; CAE03579.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16085.2; -; Genomic_DNA.
DR EMBL; AP014960; BAS91492.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ32318.1; -; Genomic_DNA.
DR RefSeq; XP_015634184.1; XM_015778698.1.
DR AlphaFoldDB; Q7XPK7; -.
DR SMR; Q7XPK7; -.
DR STRING; 4530.OS04T0664600-00; -.
DR PaxDb; Q7XPK7; -.
DR PRIDE; Q7XPK7; -.
DR EnsemblPlants; Os04t0664600-00; Os04t0664600-00; Os04g0664600.
DR GeneID; 4337311; -.
DR Gramene; Os04t0664600-00; Os04t0664600-00; Os04g0664600.
DR KEGG; osa:4337311; -.
DR eggNOG; ENOG502QTU2; Eukaryota.
DR HOGENOM; CLU_014546_6_2_1; -.
DR InParanoid; Q7XPK7; -.
DR OMA; VEHEHRN; -.
DR OrthoDB; 1130893at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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:UniProtKB.
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..449
FT /note="Agmatine hydroxycinnamoyltransferase 1"
FT /id="PRO_0000437773"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT CONFLICT 302
FT /note="L -> P (in Ref. 5; EAZ32318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 48604 MW; 82CB5E102DAE3357 CRC64;
MKITVHSSKA VKPVYGDAVA APSTADVVPL SVFDRANFDT YVSVIYAFRP PAPANSVLEA
GLAKALAEYR EWAGRLGVDG DGDRAILLND AGARFVEATA DVTLDSVVPL EPTPRVTSLH
PSADDDGAEA EVMMVQVTRF ACGSLAVGFT AHHMVSDGRA TSNFFLAWSQ ATRGVAIHPV
PVHDRASFFT PRDPPRVDYE HRGVEFKTCE KLDRNENNDD GHGHGHDGEV VVTHKVHFSR
EFISKLKALA SAGGGQRSYS TLQCVVAHLW RCITMARGLE GSVATSVSIA VDGRARMSPP
VLDGYTGNVV LWARPTATAR ELVTMPLQHA MGLINRAVAR INDGYFKSFV DFANSGAVEE
ERLVASADAA EMVLSPNIEV DSWLRIPFYE LDFGSGQPFL FTPSYLPVEG LLILLPSFSG
DGSVDAYVPL FSHDMDTFKN CCYVLPELS
