Tag | Content |
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CPLM ID | CPLM-004485 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ferrochelatase, mitochondrial |
Protein Synonyms/Alias | Heme synthase; Protoheme ferro-lyase |
Gene Name | HEM15 |
Gene Synonyms/Alias | YOR176W |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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81 | KYQKTIAKYIAKFRT | acetylation | [1] | 130 | CPETAPHKPYVAFRY | acetylation | [1] | 147 | PLTAETYKQMLKDGV | acetylation | [1] | 381 | GKSNDPVKDLSLVFG | acetylation | [1] |
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Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Catalyzes the ferrous insertion into protoporphyrin IX. |
Sequence Annotation | ACT_SITE 351 351 By similarity. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Heme biosynthesis; Iron; Lyase; Membrane; Mitochondrion; Mitochondrion inner membrane; Porphyrin biosynthesis; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 393 AA |
Protein Sequence | MLSRTIRTQG SFLRRSQLTI TRSFSVTFNM QNAQKRSPTG IVLMNMGGPS KVEETYDFLY 60 QLFADNDLIP ISAKYQKTIA KYIAKFRTPK IEKQYREIGG GSPIRKWSEY QATEVCKILD 120 KTCPETAPHK PYVAFRYAKP LTAETYKQML KDGVKKAVAF SQYPHFSYST TGSSINELWR 180 QIKALDSERS ISWSVIDRWP TNEGLIKAFS ENITKKLQEF PQPVRDKVVL LFSAHSLPMD 240 VVNTGDAYPA EVAATVYNIM QKLKFKNPYR LVWQSQVGPK PWLGAQTAEI AEFLGPKVDG 300 LMFIPIAFTS DHIETLHEID LGVIGESEYK DKFKRCESLN GNQTFIEGMA DLVKSHLQSN 360 QLYSNQLPLD FALGKSNDPV KDLSLVFGNH EST 393 |
Gene Ontology | GO:0005743; C:mitochondrial inner membrane; IDA:SGD. GO:0004325; F:ferrochelatase activity; IDA:SGD. GO:0006783; P:heme biosynthetic process; IMP:SGD. |
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