Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.75
Description:Uroporphyrinogen-III synthase.
Alternative Name: Uroporphyrinogen-III cosynthetase.
Uroporphyrinogen-III cosynthase.
Hydroxymethylbilane hydro-lyase (cyclizing).
Cath: 3.30.160.40; 3.40.190.10; 3.40.50.10090;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.75
BRENDA Enzyme Link: BRENDA 4.2.1.75
KEGG Enzyme Link: KEGG4.2.1.75
BioCyc Enzyme Link: BioCyc 4.2.1.75
ExPASy Enzyme Link: ExPASy4.2.1.75
EC2PDB Enzyme Link: EC2PDB 4.2.1.75
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.75
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.75
IntEnz Enzyme Link: IntEnz 4.2.1.75
MEDLINE Enzyme Link: MEDLINE 4.2.1.75
MSA:

4.2.1.75;

Phylogenetic Tree:

4.2.1.75;

Uniprot:
M-CSA:
RHEA:18965 hydroxymethylbilane = H2O + uroporphyrinogen III
RULE(radius=1)
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification and properties of uroporphyrinogen III synthase from human erythrocytes.Tsai SF, Bishop DF, Desnick RJ1987 Jan 253805019
Bacterial heme biosynthesis and its biotechnological application.Frankenberg N, Moser J, Jahn D2003 Dec13680202
Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase.Schubert HL, Raux E, Matthews MA, Phillips JD, Wilson KS, Hill CP, Warren MJ2002 Aug12196144
Crystal structure of human uroporphyrinogen III synthase.Mathews MA, Schubert HL, Whitby FG, Alexander KJ, Schadick K, Bergonia HA, Phillips JD, Hill CP2001 Nov 111689424
Biosynthesis of the pigments of life: formation of the macrocycle.Battersby AR, Fookes CJ, Matcham GW, McDonald E1980 May 16769048