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
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
Structural insight into human variegate porphyria disease.
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1.9 Angstrom crystal structure of human PPO in complex with FAD and the inhibitor acifluorfen; hPPO converts protoporphyrinogen IX to protoporphyrin IX and is a mitochondrial inner membrane protein. Also characterised 47 VP-causing mutants.
"Human protoporphyrinogen IX oxidase (hPPO), a mitochondrial inner membrane protein, converts protoporphyrinogen IX to protoporphyrin IX in the heme biosynthetic pathway."
Quantitative structural insight into human variegate porphyria disease.
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PPO (EC 1.3.3.4) is the penultimate enzyme of heme biosynthesis, oxidising protoporphyrinogen IX to protoporphyrin IX using FAD and molecular oxygen; ~50% decreased activity causes dominantly inherited variegate porphyria (an acute hepatic porphyria).
"catalyzes the oxidation of protoporphyrinogen IX (protogen) to protoporphyrin IX (porphyrin) in the presence of cofactor FAD and molecular oxygen"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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Large-scale proteomic study defining a high-confidence human mitochondrial proteome (MitoCoP) of >1,100 proteins, supporting mitochondrial localisation of PPOX.
"defined a mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP)"
Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli.
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Cloning of the human PPOX cDNA by complementation of an E. coli hemG (PPO-deficient) mutant; PPO is the penultimate heme-pathway enzyme, a mitochondrial flavoprotein whose activity is inhibited by acifluorfen.
"Protoporphyrinogen oxidase (PPO; EC 1.3.3.4) is the enzyme that catalyzes in the penultimate step in the heme biosynthetic pathway."
PPO oxidises PPGEN9 to PRIN9
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Reactome reaction: six-electron oxidation of protoporphyrinogen IX to protoporphyrin IX by PPO, a FAD-containing enzyme on the outer surface of the inner mitochondrial membrane; PPO deficiency causes variegate porphyria.
"The protein resides on the outer surface of the inner mitochondrial membrane."
UniProtKB entry P50336 (PPOX_HUMAN)
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UniProt records the catalytic reaction (protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2; EC 1.3.3.4), FAD cofactor (one per subunit), mitochondrial inner membrane peripheral (intermembrane-side) localisation, and the disease associations variegate porphyria and childhood-onset variegate porphyria.
"Reaction=protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2;"