Sequence of Q9U8X2_ENTHI
EC Number:2.3.1.30
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Other sequences found for EC No. 2.3.1.30
General information:
Sequence
0 MDNYIYSIAH QLYEMYLQDE DAFHSKRDYP HKKVFTELQK LRKIFFPDFF MKHQKITESH
60 IASELTKLVD YIKDSVTAYN DELFAHQCVM AILEKLPSIK RTLKTDLIAA YAGDPAAPGL
120 SLIIRCYPGF QAVIVYRIAH VLYECGERYY CREMMESVHS YTSIDIHPGA SIKGHFFIDH
180 GVGVVIGETA IIGEWCRIYQ SVTLGAMHFQ EEGGVIKRGT KRHPTVGDYV TIGTGAKVLG
240 NIIVGSHVRI GANCWIDRDV DSNQTVYISE HPTHFVKPCT TKGMKNDTEI IAIIPSSPLA
300 NSPSI
Download this sequence
in fasta formatDownload all sequences for 2.3.1.30
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
72824285
Nozaki T.,Asai T.,Sanchez L.B.,Kobayashi S.,Nakazawa M.,Takeuchi T.
Characterization of the gene encoding serine acetyltransferase, a regulated enzyme of cysteine biosynthesis from the protist parasites Entamoeba histolytica and Entamoeba dispar. Regulation and possible function of the cysteine biosynthetic pathway in Entamoeba.
J. Biol. Chem.
274
32445-32452
1999
72824286
Kumar S.,Raj I.,Nagpal I.,Subbarao N.,Gourinath S.
Structural and biochemical studies of serine acetyltransferase reveal why the parasite Entamoeba histolytica cannot form a cysteine synthase complex.
J. Biol. Chem.
286
12533-12541
2011
