Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Crystal structure of human uroporphyrinogen III synthase.
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Human U3S catalyzes ring closure of the linear tetrapyrrole hydroxymethylbilane with concurrent flipping of the D ring to form uroporphyrinogen III; it is the fourth enzyme of the porphyrin biosynthetic pathway and exists as a monomer.
"catalyzes ring closure of the linear tetrapyrrole hydroxymethylbilane (HMB), with concurrent flipping of the D ring"
Human uroporphyrinogen III synthase: NMR-based mapping of the active site.
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URO-synthase catalyzes the cyclization and D-ring isomerization of hydroxymethylbilane to uroporphyrinogen III; it is a cytosolic enzyme of heme biosynthesis whose deficiency causes congenital erythropoietic porphyria.
"cytosolic enzymes of heme biosynthesis"
Human uroporphyrinogen III synthase: molecular cloning, nucleotide sequence, and expression of a full-length cDNA.
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Cloning and E. coli expression of full-length human URO-synthase cDNA encoding a 265-aa protein; the enzyme is the fourth enzyme of the heme biosynthetic pathway that converts hydroxymethylbilane to uroporphyrinogen III.
"the cyclic tetrapyrrole, uroporphyrinogen III"
Purification and properties of uroporphyrinogen III synthase from human erythrocytes.
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UROS was purified to homogeneity from human erythrocytes and, using hydroxymethylbilane as substrate, formed uroporphyrinogen III without hydroxymethylbilane synthase or other cofactors; the enzyme is a monomer.
"the purified enzyme formed uroporphyrinogen"
Heme biosynthesis
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Heme biosynthesis proceeds via eight enzymes, four in the cytosol; four molecules of PBG are converted into the cyclic tetrapyrrole uroporphyrinogen III.
"The next two steps convert four molecules of PBG into the cyclic tetrapyrrole uroporphyringen III"
UROS transforms HMB to URO3
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Cytosolic UROS catalyzes conversion of hydroxymethylbilane to uroporphyrinogen III via ring closure and intramolecular rearrangement; uroporphyrinogen III is the branch point for heme, chlorophyll and corrins.
"catalyzes the conversion of HMB (hydroxymethylbilane) to uroporphyrinogen III, a reaction involving ring"
UniProtKB entry P10746 (HEM4_HUMAN), Uroporphyrinogen-III synthase
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UROS catalyzes cyclization of the linear tetrapyrrole hydroxymethylbilane to the macrocyclic uroporphyrinogen III, the branch point for the porphyrin sub-pathways; it is a cytosolic monomer, and deficiency causes congenital erythropoietic porphyria with non-enzymatic conversion of hydroxymethylbilane to the uroporphyrinogen-I isomer.
"Catalyzes cyclization of the linear tetrapyrrole,"