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Enzyme Name | UniProtKB | KEGG |
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| P21631 | Q5SKH6 | Q53WA2 |
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Protein name | Uroporphyrinogen-III C-methyltransferase |
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| uroporphyrinogen-III C-methyltransferaseuroporphyrinogen methyltransferaseuroporphyrinogen-III methyltransferaseadenosylmethionine-uroporphyrinogen III methyltransferaseS-adenosyl-L-methionine-dependent uroporphyrinogen III methylaseuroporphyrinogen-III methylaseSirACysGCobA [ambiguous - see EC 2.5.1.17] SUMTuroporphyrin-III C-methyltransferase (incorrect)S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase(incorrect) |
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Synonyms | Urogen III methylaseEC 2.1.1.107SUMTUroporphyrinogen III methylaseUROM | Putative uncharacterized protein TTHA0667 | S-adenosyl-L-methionine uroporphyrinogen methyltransferase |
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RefSeq |
| YP_143933.1 (Protein) NC_006461.1 (DNA/RNA sequence)
| YP_145299.1 (Protein) NC_006462.1 (DNA/RNA sequence)
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Pfam | PF00590 (TP_methylase) [Graphical view]
| PF00590 (TP_methylase) [Graphical view]
| PF00590 (TP_methylase) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00860 | Porphyrin and chlorophyll metabolism |
UniProtKB:Accession Number | P21631 | Q5SKH6 | Q53WA2 |
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Entry name | SUMT_PSEDE | Q5SKH6_THET8 | Q53WA2_THET8 |
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Activity | S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.,S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2. | S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2.,S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. | S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2.,S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. |
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Subunit | Homodimer. |
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Subcellular location |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00019 | C01051 | C15527 | C00021 | C15527 | C02463 |
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Compound | S-Adenosyl-L-methionine | Uroporphyrinogen III | Precorrin 1 | S-Adenosyl-L-homocysteine | Precorrin 1 | Precorrin 2 |
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Type | amino acids,amine group,nucleoside,sulfonium ion | aromatic ring (with nitrogen atoms),carboxyl group | aromatic ring (with nitrogen atoms),carboxyl group | amino acids,amine group,nucleoside,sulfide group | aromatic ring (with nitrogen atoms),carboxyl group | amine group,aromatic ring (with nitrogen atoms),carboxyl group |
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ChEBI | 67040
| 15437
| 52469
| 16680 57856
| 52469
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PubChem | 34755
| 1179
| 11954200
| 439155 25246222
| 11954200
| 5280516
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| | | | | | | | | | | | | |
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1s4dA01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dB01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dD01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dE01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dF01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dG01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dH01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dI01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dJ01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dK01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dL01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dM01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1v9aA01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1v9aB01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1va0A01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1va0B01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1ve2A01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1ve2B01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1s4dA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dD02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dE02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dF02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dG02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dH02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dI02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dJ02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dK02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dL02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1s4dM02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1v9aA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1v9aB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound |
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1va0A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1va0B02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1ve2A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1ve2B02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[4] | p.588-589 |
| [9] | p.1068-1069 |
| [10] | Fig.1, p.429-430 |
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references | [1] |
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Comments | CHARACTERIZATION. |
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PubMed ID | 2546914 |
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Journal | J Bacteriol |
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Year | 1989 |
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Volume | 171 |
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Pages | 4222-31 |
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Authors | Blanche F, Debussche L, Thibaut D, Crouzet J, Cameron B |
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Title | Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificans. |
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Related UniProtKB | P21631 |
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[2] |
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PubMed ID | 1508200 |
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Journal | Mol Cell Biol |
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Year | 1992 |
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Volume | 12 |
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Pages | 4026-37 |
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Authors | Mattheakis LC, Shen WH, Collier RJ |
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Title | DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae. |
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[3] |
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PubMed ID | 8501034 |
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Journal | J Bacteriol |
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Year | 1993 |
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Volume | 175 |
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Pages | 3303-16 |
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Authors | Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM |
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Title | Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. |
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[4] |
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PubMed ID | 9461500 |
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Journal | Biochem J |
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Year | 1998 |
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Volume | 330 |
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Pages | 121-9 |
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Authors | Woodcock SC, Raux E, Levillayer F, Thermes C, Rambach A, Warren MJ |
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Title | Effect of mutations in the transmethylase and dehydrogenase/chelatase domains of sirohaem synthase (CysG) on sirohaem and cobalamin biosynthesis. |
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[5] |
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Comments | X-ray crystallography |
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PubMed ID | 9665173 |
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Journal | Nat Struct Biol |
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Year | 1998 |
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Volume | 5 |
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Pages | 585-92 |
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Authors | Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ |
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Title | The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. |
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Related PDB | 1cbf,2cbf |
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[6] |
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PubMed ID | 10400331 |
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Journal | Bioorg Med Chem |
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Year | 1999 |
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Volume | 7 |
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Pages | 789-94 |
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Authors | Santander PJ, Stolowich NJ, Scott AI |
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Title | Chemoenzymatic synthesis of an unnatural tetramethyl cobalt corphinoid. |
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[7] |
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PubMed ID | 12195810 |
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Journal | Nat Prod Rep |
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Year | 2002 |
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Volume | 19 |
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Pages | 390-412 |
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Authors | Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC |
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Title | The biosynthesis of adenosylcobalamin (vitamin B12). |
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[8] |
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PubMed ID | 12662021 |
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Journal | J Org Chem |
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Year | 2003 |
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Volume | 68 |
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Pages | 2529-39 |
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Authors | Scott AI |
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Title | Discovering nature's diverse pathways to vitamin B12: a 35-year odyssey. |
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[9] |
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Comments | X-ray crystallography |
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PubMed ID | 14595395 |
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Journal | Nat Struct Biol |
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Year | 2003 |
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Volume | 10 |
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Pages | 1064-73 |
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Authors | Stroupe ME, Leech HK, Daniels DS, Warren MJ, Getzoff ED |
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Title | CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis. |
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Related PDB | 1pjq,1pjs,1pjt |
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[10] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF APOPROTEIN IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, SUBUNIT, KINETIC PARAMETERS, AND MUTAGENESIS OF ASP-47; LEU-49; PHE-106; THR-130; TYR-183 AND MET-184. |
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PubMed ID | 15522295 |
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Journal | J Mol Biol |
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Year | 2004 |
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Volume | 344 |
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Pages | 419-33 |
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Authors | Vevodova J, Graham RM, Raux E, Schubert HL, Roper DI, Brindley AA, Ian Scott A, Roessner CA, Stamford NP, Elizabeth Stroupe M, Getzoff ED, Warren MJ, Wilson KS |
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Title | Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis. |
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Related PDB | 1s4d |
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Related UniProtKB | P21631 |
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[11] |
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Comments | X-ray crystallography |
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PubMed ID | 15983414 |
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Journal | Acta Crystallogr D Biol Crystallogr |
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Year | 2005 |
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Volume | 61 |
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Pages | 913-9 |
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Authors | Rehse PH, Kitao T, Tahirov TH |
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Title | Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus. |
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Related PDB | 1v9a,1va0 |
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[12] |
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Comments | X-ray crystallography |
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PubMed ID | 17229157 |
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Journal | FEBS J |
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Year | 2007 |
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Volume | 274 |
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Pages | 563-73 |
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Authors | Wada K, Harada J, Yaeda Y, Tamiaki H, Oh-Oka H, Fukuyama K |
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Title | Crystal structures of CbiL, a methyltransferase involved in anaerobic vitamin B biosynthesis, and CbiL in complex with S-adenosylhomocysteine - implications for the reaction mechanism. |
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Related PDB | 2e0k,2e0n |
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comments | According to the literature [10], this enzyme catalyzes the following reactions: (A) Transfer of methyl group from the sulfur atom of SAM to the C2 (sp2 carbon) of uroporphyrinogen III: (B) Isomerization; Shift of double-bond position (from N=C-C to N-C=C): (C) Isomerization; Shift of double-bond position (from C=C-C to C-C=C), forming precorrin-1: (D) Transfer of methyl group from the sulfur atom of SAM to the C7 (sp2 carbon) of precorrin-1: (E) Isomerization; Shift of double-bond position (from N=C-C to N-C=C): (F) Isomerization; Shift of double-bond position (from C=C-C to C-C=C), producing precorrin-2: ### During the following reactions, Asp47 (PDB;1s4d) acts as a general base to deprotonate the C5 or C10 methylene. (C) Isomerization; Shift of double-bond position (from C=C-C to C-C=C), forming precorrin-1: (F) Isomerization; Shift of double-bond position (from C=C-C to C-C=C), producing precorrin-2:
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created | updated |
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2007-02-19 | 2009-04-03 |
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