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Enzyme Name | UniProtKB | KEGG |
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| O29537 |
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Protein name | Sirohydrochlorin cobaltochelatase | Sirohydrochlorin cobaltochelataseCbiXCbiXSAnaerobic cobalt chelataseCobaltochelatase [ambiguous]Sirohydrochlorin cobalt-lyase (incorrect) |
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Synonyms | EC 4.99.1.3CbiXS |
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RefSeq | NP_069555.1 (Protein) NC_000917.1 (DNA/RNA sequence)
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Pfam | PF01903 (CbiX) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00860 | Porphyrin and chlorophyll metabolism |
UniProtKB:Accession Number | O29537 |
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Entry name | CBIX_ARCFU |
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Activity | Sirohydrochlorin + Co(2+) = cobalt-sirohydrochlorin + 2 H(+). |
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Subunit | Tetramer. |
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Subcellular location |
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Cofactor |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[7] | Fig.1, p.38 |
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references | [1] |
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PubMed ID | 11215515 |
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Journal | Cell Mol Life Sci |
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Year | 2000 |
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Volume | 57 |
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Pages | 1880-93 |
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Authors | Raux E, Schubert HL, Warren MJ |
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Title | Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum. |
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[2] |
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PubMed ID | 11007789 |
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Journal | J Biol Chem |
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Year | 2000 |
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Volume | 275 |
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Pages | 40316-23 |
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Authors | Roper JM, Raux E, Brindley AA, Schubert HL, Gharbia SE, Shah HN, Warren MJ |
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Title | The enigma of cobalamin (Vitamin B12) biosynthesis in Porphyromonas gingivalis. Identification and characterization of a functional corrin pathway. |
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[3] |
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PubMed ID | 12408752 |
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Journal | Biochem J |
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Year | 2003 |
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Volume | 370 |
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Pages | 505-16 |
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Authors | Raux E, Leech HK, Beck R, Schubert HL, Santander PJ, Roessner CA, Scott AI, Martens JH, Jahn D, Thermes C, Rambach A, Warren MJ |
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Title | Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium. |
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[4] |
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PubMed ID | 12758040 |
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Journal | Green or red: what stops the traffic in the tetrapyrrole pathway? Trends Plant Sci |
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Year | 2003 |
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Volume | 8 |
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Pages | 224-30 |
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Authors | Cornah JE, Terry MJ, Smith AG |
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Title |
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[5] |
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PubMed ID | 12686546 |
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Journal | J Biol Chem |
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Year | 2003 |
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Volume | 278 |
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Pages | 22388-95 |
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Authors | Brindley AA, Raux E, Leech HK, Schubert HL, Warren MJ |
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Title | A story of chelatase evolution: identification and characterization of a small 13-15-kDa "ancestral" cobaltochelatase (CbiXS) in the archaea. |
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[6] |
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PubMed ID | 12869542 |
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Journal | J Biol Chem |
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Year | 2003 |
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Volume | 278 |
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Pages | 41148-59 |
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Authors | Rodionov DA, Vitreschak AG, Mironov AA, Gelfand MS |
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Title | Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes. |
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[7] |
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PubMed ID | 16835730 |
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Journal | J Struct Funct Genomics |
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Year | 2006 |
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Volume | 7 |
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Pages | 37-50 |
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Authors | Yin J, Xu LX, Cherney MM, Raux-Deery E, Bindley AA, Savchenko A, Walker JR, Cuff ME, Warren MJ, James MN |
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Title | Crystal structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS, from Archaeoglobus fulgidus. |
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Related PDB | 1tjn,2dj5 |
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[8] |
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PubMed ID | 17584754 |
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Journal | Protein Eng Des Sel |
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Year | 2007 |
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Volume | 20 |
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Pages | 257-65 |
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Authors | Pisarchik A, Petri R, Schmidt-Dannert C |
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Title | Probing the structural plasticity of an archaeal primordial cobaltochelatase CbiX(S). |
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[9] |
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PubMed ID | 21173279 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 2011 |
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Volume | 108 |
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Pages | 97-102 |
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Authors | Romao CV, Ladakis D, Lobo SA, Carrondo MA, Brindley AA, Deery E, Matias PM, Pickersgill RW, Saraiva LM, Warren MJ |
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Title | Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization. |
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Related PDB | 2xwq,2xws,2xwp,2xvx,2xvz |
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comments | This enzyme forms a homodimer with a symmetrical active site, which is located at the interface of the two subunits (see [9]). This enzyme (CbiXS) can be an ancestral enzyme of CbiK (D00828 in EzCatDB) (see [9]). According to the literature [9], this enzyme catalyzes the insertion of cobalt ion into a tetra-pyrrole, sirohydrochlorin (SHC). This reaction involves several steps including removal of water from the metal ion, deprotonation of the tetra-pyrrole nitrogens (see [9]). The distortion of the tetra-pyrrole during the reaction is smaller than that caused in the homologous enzyme, CbiK (see [9]). The lack of distortion can be compensated by the fact that either face of the bound SHC can be deprotonated. If the cobalt is bound to a subunit of the dimer, then His10 on the other subunit can deprotonate the pyrrole nitrogen. Moreover, a metal-oxygen bond with the propionate group of either A or B ring on SHC might stabilize the metal-insertion reaction (see [9]).
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created | updated |
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2009-11-06 | 2011-11-07 |
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