Sequence of HST_ARATH
EC Number:2.3.1.133
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate
Other sequences found for EC No. 2.3.1.133
General information:
Sequence
0 MKINIRDSTM VRPATETPIT NLWNSNVDLV IPRFHTPSVY FYRPTGASNF FDPQVMKEAL
60 SKALVPFYPM AGRLKRDDDG RIEIDCNGAG VLFVVADTPS VIDDFGDFAP TLNLRQLIPE
120 VDHSAGIHSF PLLVLQVTFF KCGGASLGVG MQHHAADGFS GLHFINTWSD MARGLDLTIP
180 PFIDRTLLRA RDPPQPAFHH VEYQPAPSMK IPLDPSKSGP ENTTVSIFKL TRDQLVALKA
240 KSKEDGNTVS YSSYEMLAGH VWRSVGKARG LPNDQETKLY IATDGRSRLR PQLPPGYFGN
300 VIFTATPLAV AGDLLSKPTW YAAGQIHDFL VRMDDNYLRS ALDYLEMQPD LSALVRGAHT
360 YKCPNLGITS WVRLPIYDAD FGWGRPIFMG PGGIPYEGLS FVLPSPTNDG SLSVAIALQS
420 EHMKLFEKFL FEI
Download this sequence
Download all sequences for 2.3.1.133
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
45197
Kaneko T.,Katoh T.,Sato S.,Nakamura Y.,Asamizu E.,Kotani H.,Miyajima N.,Tabata S.
Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones.
DNA Res.
6
183-195
1999
45198
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
45202
Hoffmann L.,Besseau S.,Geoffroy P.,Ritzenthaler C.,Meyer D.,Lapierre C.,Pollet B.,Legrand M.
Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis.
Plant Cell
16
1446-1465
2004
45203
Eudes A.,Pereira J.H.,Yogiswara S.,Wang G.,Teixeira Benites V.,Baidoo E.E.K.,Lee T.S.,Adams P.D.,Keasling J.D.,Loque D.
Exploiting the substrate promiscuity of hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl transferase to reduce lignin.
Plant Cell Physiol.
57
568-579
2016
45204
Levsh O.,Chiang Y.-C.,Tung C.F.,Noel J.P.,Wang Y.,Weng J.-K.
Dynamic conformational states dictate selectivity toward the native substrate in a substrate-permissive acyltransferase.
Biochemistry
55
6314-6326
2016