Literature summary for 3.5.4.25 extracted from

Singh, M.; Kumar, P.; Karthikeyan, S.
Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis (2011), J. Struct. Biol., 174, 374-384.

Search for more literature for 3.5.4.25

Cloned(Commentary)

Cloned (Comment)	Organism
gene ribA2, DNA and amino acid sequence analysis and comparison of DHBPS/GTPCH-II sequences	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	single gene ribA2 or Rv1415, encodes for the bifunctional enzyme with DHBPS and GTPCH-II domains	-

Synonyms

Synonyms	Comment	Organism
GTP cyclohydrolase-II	-	Mycobacterium tuberculosis
GTPCH-II	-	Mycobacterium tuberculosis
guanosine-5'-triphosphate cyclohydrolase-II	-	Mycobacterium tuberculosis

General Information

General Information	Comment	Organism
metabolism	3,4-dihydroxy 2-butanone 4-phosphate synthase, DHBPS EC 4.1.99.12, and GTP cyclohydrolase-II, GTPCH-II, are the two initial enzymes involved in riboflavin biosynthesis pathway, which is essential for the pathogen	Mycobacterium tuberculosis
additional information	bifunctional enzyme with 3,4-dihydroxy 2-butanone 4-phosphate synthase, DHBPS EC 4.1.99.12, and GTP cyclohydrolase-II, GTPCH-II, domains at N- and C-termini, respectively	Mycobacterium tuberculosis
physiological function	3,4-dihydroxy 2-butanone 4-phosphate synthase, DHBPS EC 4.1.99.12, and GTP cyclohydrolase-II, GTPCH-II, are the two initial enzymes involved in riboflavin biosynthesis pathway, which is essential for the pathogen	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)