P22600 (HEMH_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 97.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ferrochelatase, mitochondrial EC=4.99.1.1 Alternative name(s): Heme synthase Protoheme ferro-lyase | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 416 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the ferrous insertion into protoporphyrin IX. |
| Catalytic activity | Protoheme + 2 H+ = protoporphyrin + Fe2+. |
| Cofactor | Binds 1 2Fe-2S cluster. |
| Enzyme regulation | Inhibited by nitric oxide (NO). The 2Fe-2S cluster could act as a NO sensor By similarity. |
| Pathway | Porphyrin metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. |
| Sequence similarities | Belongs to the ferrochelatase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Heme biosynthesis Porphyrin biosynthesis |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Transit peptide |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ferrochelatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 47 | 47 | Mitochondrion Potential | ||||||
| Chain | 48 – 416 | 369 | Ferrochelatase, mitochondrial | PRO_0000008872 | |||||
Sites | |||||||||
| Active site | 223 | 1 | By similarity | ||||||
| Active site | 376 | 1 | By similarity | ||||||
| Metal binding | 189 | 1 | Iron-sulfur (2Fe-2S) | ||||||
| Metal binding | 396 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 399 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 404 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 282 | 1 | D → E AA sequence Ref.2 | ||||||
| Sequence conflict | 287 | 1 | S → P AA sequence Ref.2 | ||||||
| Sequence conflict | 287 | 1 | S → P AA sequence Ref.3 | ||||||
Sequences
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References
| [1] | "The coding sequence of the bovine ferrochelatase gene." Shibuya H., Nonneman D., Tamassia M., Allphin O.L., Johnson G.S. Biochim. Biophys. Acta 1231:117-120(1995) [PubMed: 7640290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning of murine ferrochelatase." Brenner D.A., Frasier F. Proc. Natl. Acad. Sci. U.S.A. 88:849-853(1991) [PubMed: 1704134] [Abstract] Cited for: PROTEIN SEQUENCE OF 281-311. Tissue: Liver. |
| [3] | "Molecular cloning, sequencing, and expression of mouse ferrochelatase." Taketani S., Nakahashi Y., Osumi T., Tokunaga R. J. Biol. Chem. 265:19377-19380(1990) [PubMed: 2246229] [Abstract] Cited for: PROTEIN SEQUENCE OF 152-157; 266-275; 284-291 AND 373-381. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L34173 mRNA. Translation: AAA79169.1. |
| IPI | IPI00701579. |
| PIR | I45890. |
| RefSeq | NP_776479.1. NM_174054.2. |
| UniGene | Bt.88608. |
3D structure databases | |
| ProteinModelPortal | P22600. |
| SMR | P22600. Positions 58-416. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P22600. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000008384; ENSBTAP00000008384; ENSBTAG00000006393. |
| GeneID | 281158. |
| KEGG | bta:281158. |
Organism-specific databases | |
| CTD | 2235. |
Phylogenomic databases | |
| eggNOG | maNOG04866. |
| GeneTree | ENSGT00390000016258. |
| HOVERGEN | HBG051898. |
| InParanoid | P22600. |
| OMA | LQKPLAW. |
| OrthoDB | EOG4GXFN0. |
| PhylomeDB | P22600. |
Family and domain databases | |
| InterPro | IPR001015. Ferrochelatase. IPR019772. Ferrochelatase_AS. [Graphical view] |
| KO | K01772. |
| PANTHER | PTHR11108. Ferrochelatase. 1 hit. |
| Pfam | PF00762. Ferrochelatase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00109. HemH. 1 hit. |
| PROSITE | PS00534. FERROCHELATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEMH_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P22600 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with