Reviewed,
UniProtKB/Swiss-Prot Q8FCW8 (CYSG_ECOL6)
Last modified
February 9, 2010.
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: Siroheme synthase Including the following 3 domains: 1- Recommended name: Uroporphyrinogen-III C-methyltransferase Short name=Urogen III methylase EC=2.1.1.107 Alternative name(s): SUMT Uroporphyrinogen III methylase Short name=UROM 2- Recommended name: Precorrin-2 dehydrogenase EC=1.3.1.76 3- Recommended name: Sirohydrochlorin ferrochelatase EC=4.99.1.4 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 457 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme By similarity. HAMAP MF_01646 |
| Catalytic activity | S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP MF_01646 S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP MF_01646 Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP MF_01646 Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP MF_01646 |
| Pathway | Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP MF_01646 Porphyrin metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. |
| Sequence similarities | Belongs to the precorrin methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cobalamin biosynthesis Porphyrin biosynthesis |
| Ligand | NAD S-adenosyl-L-methionine |
| Molecular function | Lyase Methyltransferase Oxidoreductase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | cobalamin biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW siroheme biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro precorrin-2 dehydrogenase activityInferred from electronic annotation. Source: HAMAP sirohydrochlorin ferrochelatase activityInferred from electronic annotation. Source: EC uroporphyrin-III C-methyltransferase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 457 | 457 | Siroheme synthase HAMAP MF_01646 | PRO_0000330510 | ||||
Regions | ||||||||
| Region | 218 – 457 | 240 | Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646 | |||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN82582.1. |
| RefSeq | NP_756008.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PJQ based on UniProtKB P25924. |
| SMR | Q8FCW8. Positions 1-457. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1036683. |
| GenomeReviews | Gene locus c4144 in contig AE014075_GR. |
| KEGG | ecc:c4144. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG730212. |
| OMA | MCRRDAE. |
Family and domain databases | |
| HAMAP | MF_01646. Siroheme_synth. [Tree] |
| InterPro | IPR000878. 4pyrrol_Mease. IPR014777. 4pyrrole_Mease_sub1. IPR014776. 4pyrrole_Mease_sub2. IPR006366. CobA_cysG_C. IPR016040. NAD(P)-bd_dom. IPR019478. Sirohaem_synthase_dimer_dom. IPR006367. Sirohaem_synthase_N. IPR003043. Uropor_MeTrfase_CS. [Graphical view] |
| Gene3D | G3DSA:3.40.1010.10. 4pyrrole_Mease_sub1. 1 hit. G3DSA:3.30.950.10. 4pyrrole_Mease_sub2. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF10414. CysG_dimeriser. 1 hit. PF00590. TP_methylase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01469. cobA_cysG_Cterm. 1 hit. TIGR01470. cysG_Nterm. 1 hit. |
| PROSITE | PS00839. SUMT_1. 1 hit. PS00840. SUMT_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYSG_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: Q8FCW8 | ||||||||
| 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


