Reviewed,
UniProtKB/Swiss-Prot O31067 (HEMN_THEVL)
Last modified
June 16, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Oxygen-independent coproporphyrinogen-III oxidase Short name=Coproporphyrinogenase Short name=Coprogen oxidase EC=1.3.99.22 | ||
| Gene names |
| ||
| Organism | Thermosynechococcus vulcanus (Synechococcus vulcanus) | ||
| Taxonomic identifier | 32053 [NCBI] | ||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Thermosynechococcus |
Protein attributes
| Sequence length | 325 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX By similarity. |
| Catalytic activity | Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine. |
| Cofactor | Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity. |
| Pathway | |
| Subunit structure | Monomer. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the anaerobic coproporphyrinogen-III oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Porphyrin biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW coproporphyrinogen dehydrogenase activityInferred from electronic annotation. Source: EC coproporphyrinogen oxidase activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 325 | ›325 | Oxygen-independent coproporphyrinogen-III oxidase | PRO_0000109953 | |||||
Sites | |||||||||
| Binding site | 13 | 1 | S-adenosyl-L-methionine 1 By similarity | ||||||
| Binding site | 40 | 1 | S-adenosyl-L-methionine 2 By similarity | ||||||
| Binding site | 52 | 1 | S-adenosyl-L-methionine 2 By similarity | ||||||
| Binding site | 77 | 1 | S-adenosyl-L-methionine 2 By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | Los D.A. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF027176 Genomic DNA. Translation: AAB84028.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.3.99.22. 276791. |
Family and domain databases | |
| InterPro | IPR006638. Elp3/MiaB/NifB. IPR004558. HemN. IPR010723. HemN_C. IPR007197. Radical_SAM. [Graphical view] |
| Pfam | PF06969. HemN_C. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view] |
| SMART | SM00729. Elp3. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00538. hemN. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HEMN_THEVL | ||||||||
| Accession | Primary (citable) accession number: O31067 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


