DB code: D00084
| CATH domain | 3.40.1010.10 : Cobalt-precorrin-4 Transmethylase; domain 1 | Catalytic domain |
|---|---|---|
| 3.30.950.10 : Methyltransferase, Cobalt-precorrin-4 Transmethylase; Domain 2 | Catalytic domain | |
| E.C. | 2.1.1.107 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam | RefSeq |
|---|---|---|---|---|
| P21631 |
Uroporphyrinogen-III C-methyltransferase
|
Urogen III methylase
EC 2.1.1.107 SUMT Uroporphyrinogen III methylase UROM |
PF00590
(TP_methylase)
[Graphical View] |
|
| Q5SKH6 |
|
Putative uncharacterized protein TTHA0667
|
PF00590
(TP_methylase)
[Graphical View] |
YP_143933.1
(Protein)
NC_006461.1 (DNA/RNA sequence) |
| Q53WA2 |
|
S-adenosyl-L-methionine uroporphyrinogen methyltransferase
|
PF00590
(TP_methylase)
[Graphical View] |
YP_145299.1
(Protein)
NC_006462.1 (DNA/RNA sequence) |
| KEGG enzyme name |
|---|
|
uroporphyrinogen-III methyltransferase
uroporphyrinogen-III C-methyltransferase uroporphyrinogen methyltransferase adenosylmethionine-uroporphyrinogen III methyltransferase S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase uroporphyrinogen-III methylase SirA CysG CobA [ambiguous - see EC 2.5.1.17] SUMT uroporphyrin-III C-methyltransferase (incorrect) S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase(incorrect) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P21631 | SUMT_PSEDE | S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2. | Homodimer. | ||
| Q5SKH6 | Q5SKH6_THET8 | S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2. S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. | |||
| Q53WA2 | Q53WA2_THET8 | S-adenosyl-L-methionine + precorrin-1 = S- adenosyl-L-homocysteine + precorrin-2. S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00860 | Porphyrin and chlorophyll metabolism |
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C00019 | C01051 | C15527 | C00021 | C15527 | C02463 | ||||||
| E.C. | ||||||||||||
| Compound | S-Adenosyl-L-methionine | Uroporphyrinogen III | Precorrin 1 | S-Adenosyl-L-homocysteine | Precorrin 1 | Precorrin 2 | ||||||
| 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 | ||||||
| ChEBI |
67040 67040 |
15437 15437 |
52469 52469 |
16680 57856 16680 57856 |
52469 52469 |
|||||||
| PubChem |
34755 34755 |
1179 1179 |
11954200 11954200 |
25246222 439155 25246222 439155 |
11954200 11954200 |
5280516 5280516 |
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| 1s4dA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dE01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dF01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dG01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dH01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dI01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dJ01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dK01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dL01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dM01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1v9aA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1v9aB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1va0A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1va0B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ve2A01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ve2B01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1s4dA02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dB02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dD02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dE02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dF02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dG02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dH02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dI02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dJ02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dK02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dL02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1s4dM02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1v9aA02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1v9aB02 |
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Unbound | Unbound | Unbound | Bound:SAH | Unbound | Unbound | |
| 1va0A02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1va0B02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ve2A02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ve2B02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [9], [10], [11] | ||
| Active-site residues | ||||||||||
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| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1s4dA01 |
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ASP 47;LYS 69 | invisible 72-73 | |||
| 1s4dB01 |
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ASP 47;LYS 69 | ||||
| 1s4dD01 |
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ASP 47; | invisible 69-73 | |||
| 1s4dE01 |
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ASP 47;LYS 69 | ||||
| 1s4dF01 |
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ASP 47;LYS 69 | invisible 70-72, side chain of K69 | |||
| 1s4dG01 |
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ASP 47;LYS 69 | ||||
| 1s4dH01 |
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ASP 47;LYS 69 | invisible side chain of K69 | |||
| 1s4dI01 |
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ASP 47;LYS 69 | invisible 73 | |||
| 1s4dJ01 |
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ASP 47;LYS 69 | invisible 70-72, side chain of K69 | |||
| 1s4dK01 |
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ASP 47;LYS 69 | invisible 73 | |||
| 1s4dL01 |
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ASP 47;LYS 69 | invisible 70, 76, side chain of K69 | |||
| 1s4dM01 |
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ASP 47;LYS 69 | invisible 73 | |||
| 1v9aA01 |
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ASP 34;LYS 54 | invisible 55-60, side chain of K54 | |||
| 1v9aB01 |
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ASP 34;LYS 54 | invisible 55-63, side chain of K54 | |||
| 1va0A01 |
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ASP 34;LYS 54 | invisible 57-60 | |||
| 1va0B01 |
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ASP 34; | invisible 53-62 | |||
| 1ve2A01 |
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ASP 35; | invisible 54-60 | |||
| 1ve2B01 |
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ASP 35; | invisible 54-63 | |||
| 1s4dA02 |
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invisible 159-165 | ||||
| 1s4dB02 |
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invisible 163 | ||||
| 1s4dD02 |
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invisible 163-166 | ||||
| 1s4dE02 |
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invisible 163-164 | ||||
| 1s4dF02 |
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invisible 159-163 | ||||
| 1s4dG02 |
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invisible 163-164 | ||||
| 1s4dH02 |
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invisible 160-166 | ||||
| 1s4dI02 |
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invisible 162-163 | ||||
| 1s4dJ02 |
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invisible 160-166 | ||||
| 1s4dK02 |
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| 1s4dL02 |
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invisible 159-163 | ||||
| 1s4dM02 |
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invisible 160-166 | ||||
| 1v9aA02 |
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| 1v9aB02 |
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| 1va0A02 |
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| 1va0B02 |
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| 1ve2A02 |
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invisible 161-166 | ||||
| 1ve2B02 |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[4]
|
p.588-589 | |
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[9]
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p.1068-1069 | |
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[10]
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Fig.1, p.429-430 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | CHARACTERIZATION. |
| Medline ID | |
| PubMed ID | 2546914 |
| Journal | J Bacteriol |
| Year | 1989 |
| Volume | 171 |
| Pages | 4222-31 |
| Authors | Blanche F, Debussche L, Thibaut D, Crouzet J, Cameron B |
| Title | Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificans. |
| Related PDB | |
| Related UniProtKB | P21631 |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1508200 |
| Journal | Mol Cell Biol |
| Year | 1992 |
| Volume | 12 |
| Pages | 4026-37 |
| Authors | Mattheakis LC, Shen WH, Collier RJ |
| Title |
DPH5, |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8501034 |
| Journal | J Bacteriol |
| Year | 1993 |
| Volume | 175 |
| Pages | 3303-16 |
| Authors | Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM |
| Title | Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9461500 |
| Journal | Biochem J |
| Year | 1998 |
| Volume | 330 |
| Pages | 121-9 |
| Authors | Woodcock SC, Raux E, Levillayer F, Thermes C, Rambach A, Warren MJ |
| Title | Effect of mutations in the transmethylase and dehydrogenase/chelatase domains of sirohaem synthase (CysG) on sirohaem and cobalamin biosynthesis. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 9665173 |
| Journal | Nat Struct Biol |
| Year | 1998 |
| Volume | 5 |
| Pages | 585-92 |
| Authors | Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ |
| Title |
The X-ray structure of a cobalamin biosynthetic enzyme, |
| Related PDB | 1cbf 2cbf |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10400331 |
| Journal | Bioorg Med Chem |
| Year | 1999 |
| Volume | 7 |
| Pages | 789-94 |
| Authors | Santander PJ, Stolowich NJ, Scott AI |
| Title | Chemoenzymatic synthesis of an unnatural tetramethyl cobalt corphinoid. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12195810 |
| Journal | Nat Prod Rep |
| Year | 2002 |
| Volume | 19 |
| Pages | 390-412 |
| Authors | Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC |
| Title | The biosynthesis of adenosylcobalamin (vitamin B12). |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12662021 |
| Journal | J Org Chem |
| Year | 2003 |
| Volume | 68 |
| Pages | 2529-39 |
| Authors | Scott AI |
| Title | Discovering nature's diverse pathways to vitamin B12: a 35-year odyssey. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 14595395 |
| Journal | Nat Struct Biol |
| Year | 2003 |
| Volume | 10 |
| Pages | 1064-73 |
| Authors | Stroupe ME, Leech HK, Daniels DS, Warren MJ, Getzoff ED |
| Title | CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis. |
| Related PDB | 1pjq 1pjs 1pjt |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF APOPROTEIN IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, |
| Medline ID | |
| PubMed ID | 15522295 |
| Journal | J Mol Biol |
| Year | 2004 |
| Volume | 344 |
| Pages | 419-33 |
| 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 |
| Title |
Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), |
| Related PDB | 1s4d |
| Related UniProtKB | P21631 |
| [11] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 15983414 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2005 |
| Volume | 61 |
| Pages | 913-9 |
| Authors | Rehse PH, Kitao T, Tahirov TH |
| Title | Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus. |
| Related PDB | 1v9a 1va0 |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 17229157 |
| Journal | FEBS J |
| Year | 2007 |
| Volume | 274 |
| Pages | 563-73 |
| Authors | Wada K, Harada J, Yaeda Y, Tamiaki H, Oh-Oka H, Fukuyama K |
| Title |
Crystal structures of CbiL, |
| Related PDB | 2e0k 2e0n |
| Related UniProtKB | |
| Comments |
|---|
|
According to the literature [10], (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), (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), ### During the following reactions, (C) Isomerization; Shift of double-bond position (from C=C-C to C-C=C), (F) Isomerization; Shift of double-bond position (from C=C-C to C-C=C), |
| Created | Updated |
|---|---|
| 2007-02-19 | 2009-04-03 |