Reviewed,
UniProtKB/Swiss-Prot P95651 (HEMN_RHOS5)
Last modified
November 25, 2008.
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 |
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| Organism | Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 349102 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter |
Protein attributes
| Sequence length | 452 AA. |
| Sequence status | Complete. |
| 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 CO(2) + 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 | CytoplasmBy 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 |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| 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 – 452 | 452 | Oxygen-independent coproporphyrinogen III oxidase | PRO_0000109949 | |||||
Regions | |||||||||
| Region | 112 – 113 | 2 | S-adenosyl-L-methionine 2 binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 60 | 1 | Iron-sulfur (4Fe-4S-S-AdoMet) By similarity | ||||||
| Metal binding | 64 | 1 | Iron-sulfur (4Fe-4S-S-AdoMet) By similarity | ||||||
| Metal binding | 67 | 1 | Iron-sulfur (4Fe-4S-S-AdoMet) By similarity | ||||||
| Binding site | 54 | 1 | S-adenosyl-L-methionine 1 By similarity | ||||||
| Binding site | 66 | 1 | S-adenosyl-L-methionine 2; via carbonyl oxygen By similarity | ||||||
| Binding site | 111 | 1 | S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 144 | 1 | S-adenosyl-L-methionine 1 By similarity | ||||||
| Binding site | 171 | 1 | S-adenosyl-L-methionine 2 By similarity | ||||||
| Binding site | 183 | 1 | S-adenosyl-L-methionine 2 By similarity | ||||||
| Binding site | 208 | 1 | S-adenosyl-L-methionine 2 By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 22 | 1 | S → C in AAB38508. Ref.1 | ||||||
| Sequence conflict | 70 | 1 | R → P in AAB38508. Ref.1 | ||||||
| Sequence conflict | 197 – 198 | 2 | LR → CA in AAB38508. Ref.1 | ||||||
| Sequence conflict | 302 | 1 | S → T in AAB38508. Ref.1 | ||||||
| Sequence conflict | 306 | 1 | R → G in AAB38508. Ref.1 | ||||||
| Sequence conflict | 356 | 1 | G → A in AAB38508. Ref.1 | ||||||
| Sequence conflict | 402 | 1 | I → L in AAB38508. Ref.1 | ||||||
| Sequence conflict | 443 | 1 | T → S in AAB38508. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Shi J., Bartnikas T.B., Shapleigh J.P. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. Kaplan S.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| U80081 Genomic DNA. Translation: AAB38508.1. CP000661 Genomic DNA. Translation: ABP69878.1. | |
| PIR | T10882. |
| RefSeq | YP_001167183.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5083193. |
| GenomeReviews | Gene locus Rsph17025_0977 in contig CP000661_GR. |
| KEGG | rsq:Rsph17025_0977. |
Organism-specific databases | |
| CMR | Search... |
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_RHOS5 | ||||||||
| Accession | Primary (citable) accession number: P95651 Secondary accession number(s): A4WR64 | ||||||||
| 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


