| http://purl.uniprot.org/citations/2185242 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2185242 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2185242 | http://www.w3.org/2000/01/rdf-schema#comment | "The HEM15 gene in Saccharomyces cerevisiae encodes ferrochelatase (EC 4.99.1.1, protoheme ferrolyase), a mitochondrial inner membrane-bound enzyme which catalyzes the insertion of ferrous ion into protoporphyrin IX, the last step in protoheme biosynthesis. The gene was isolated by functional complementation of a hem15 mutant. Sequence analysis of a 2.9-kilobase genomic DNA fragment revealed an open reading frame of 1179 nucleotides, plus a gene coding for a tRNA(Val)(GUU) and delta elements downstream from the 3'-end of HEM15. The open reading frame encodes a precursor form of the protein containing a 31-amino acid presequence. The mature enzyme contains 362 amino acid residues; its calculated molecular weight (40,900) and predicted amino-terminal sequence agree with those determined from the purified protein. It is relatively abundant in lysine (9%) and contains no apparent transmembrane segment. Disruption of the HEM15 gene led to non-viable cells in certain genetic background. Northern (RNA) analysis showed a slight (1.5-2-fold) repression of HEM15 expression by glucose."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)39111-2"xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)39111-2"xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/author | "Labbe-Bois R."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/author | "Labbe-Bois R."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/pages | "7278-7283"xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/pages | "7278-7283"xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/title | "The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/title | "The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15."xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/volume | "265"xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://purl.uniprot.org/core/volume | "265"xsd:string |
| http://purl.uniprot.org/citations/2185242 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2185242 |
| http://purl.uniprot.org/citations/2185242 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2185242 |
| http://purl.uniprot.org/citations/2185242 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2185242 |
| http://purl.uniprot.org/citations/2185242 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2185242 |
| http://purl.uniprot.org/uniprot/P16622 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2185242 |
| http://purl.uniprot.org/uniprot/#_P16622-citation-2185242 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/2185242 |