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B6db families: 2.6.1.52.a

2.6.1.52 a
Activity 2.6.1.52
Description Phosphoserine aminotransferase (family a)
Notes The phosphoserine aminotransferase activity (and the associated enzymes) are diffused in a great variety of organisms. The enzyme sequences are sufficiently similar to each other to be included in a single family, but the gene genealogies are rather confuse.

This family includes only two archaeal sequences, which are very similar to eubacterial (gram +) enzymes, possibly due to a recent horizontal gene transfer. In methanococcales a broad-specificity aminotransferase seems able to carry out the transamination of phosphoserine, as well as those of aspartate, glutamate, alanine, and cysteate (Helgadóttir et al., 2007, J Bacteriol 189(2):575-82). The sequences of these archaeal enzymes are most similar to those of alanine-glyoxylate aminotransferases (EC 2.6.1.51) and may be grouped in an independent family as soon as their substrate specificity becomes better defined.

PDB 1BT4;1BJO;1BJN;6CZX;5F8V;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Reference sequence SERC_ECOLI
Domain interval 3-349
Catalytic site 198 K
 
References
 Haque MR, Hirowatari A, Koyanagi A, Ichinose T, Abiru M, Mohri S, Furuya S, Yamamoto K (2019) Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori Arch Insect Biochem Physiol 101 e21553.

 Sekula B, Ruszkowski M, Dauter Z (2018) Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) From Arabidopsis thaliana- the Enzyme Involved in the Phosphorylated Pathway of Serine Biosynthesis Front Plant Sci 6 876.

 Singh RK, Mazumder M, Sharma B, Gourinath S (2016) Structural investigation and inhibitory response of halide on phosphoserine aminotransferase from Trichomonas vaginalis Biochim Biophys Acta 1860 1508-18.

 Ali V, Nozaki T. (2006) Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways Mol Biochem Parasitol 145 :71-83.

 Dubnovitsky A.P.; Kapetaniou, E.G.; Papageorgiou, A.C. (2005) Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus Protein Sci 14 97-110.

 Baek, J.Y.; Jun do, Y.; Taub, D.; Kim, Y.H. (2003) Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis Biochem J 373 191-200.

 Hester, G.; Stark, W.; Moser, M.; Kallen, J.; Markovic-Housley, Z.; Jansonius, J. N. (1999) Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate J Mol Biol 286 829-50.

 Saito, K.; Takagi, Y.; Ling, H.C.; Takahashi, H.; Noji, M. (1997) Molecular cloning, characterization and expression of cDNA encoding phosphoserine aminotransferase involved in phosphorylated pathway of serine biosynthesis from spinach Plant Mol Biol 33 359-66.

 Battchikova, N.; Himanen, J. P.; Ahjolahti, M.; Korpela, T. (1996) Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing Biochim Biophys Acta 1295 187-94.

 Metcalf, W.W.; Zhang, J.K.; Shi, X.; Wolfe, R.S. (1996) Molecular, genetic, and biochemical characterization of the serC gene of Methanosarcina barkeri Fusaro J Bacteriol 178 5797-802.

Articles on 2.6.1.52.a
last changed 2020/02/20 09:53

B6db families