{PDOC00810} {PS01057; SAICAR_SYNTHETASE_1} {PS01058; SAICAR_SYNTHETASE_2} {BEGIN} ******************************** * SAICAR synthetase signatures * ******************************** Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) catalyzes the seventh step in the de novo purine biosynthetic pathway; the ATP-dependent conversion of 5'-phosphoribosyl-5-aminoimidazole-4- carboxylic acid and aspartic acid to SAICAR [1]. In bacteria (gene purC), fungi (gene ADE1) and plants, SAICAR synthetase is a monofunctional protein; in higher vertebrates it is the N-terminal domain of a bifunctional enzyme that also catalyze phosphoribosylaminoimidazole carboxylase (AIRC) activity. As signature patterns for SAICAR synthetase, we selected two conserved regions in the central section of this enzyme. -Consensus pattern: [LIVMRPA]-[LIVFY]-[PLNRKG]-[LIVMF]-E-x-[IV]-[LVCATI]-R- x(3)-[TAEYSI]-G-[ST] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [LI]-[IVCAP]-D-x-K-[LIFY]-E-[FI]-G -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Zalkin H., Dixon J.E. "De novo purine nucleotide biosynthesis." Prog. Nucleic Acid Res. Mol. Biol. 42:259-287(1992). PubMed=1574589 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}