Protein Domain : IPR006362

Type:  Domain Name:  Cobalamin (vitamin B12) biosynthesis CobM/CbiF, precorrin-4 C11-methyltransferase
Description:  Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants and fungi do not appear to use it. In bacteria and archaea, these include methionine synthase, ribonucleotide reductase, glutamate and methylmalonyl-CoA mutases, ethanolamine ammonia lyase, and diol dehydratase []. In mammals, cobalamin is obtained through the diet, and is required for methionine synthase and methylmalonyl-CoA mutase []. There are at least two distinct cobalamin biosynthetic pathways in bacteria []:Aerobic pathway that requires oxygen and in which cobalt is inserted late in the pathway []; found in Pseudomonas denitrificansand Rhodobacter capsulatus.Anaerobic pathway in which cobalt insertion is the first committed step towards cobalamin synthesis [, ]; found in Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii. Either pathway can be divided into two parts: (1) corrin ring synthesis (differs in aerobic and anaerobic pathways) and (2) adenosylation of corrin ring, attachment of aminopropanol arm, and assembly of the nucleotide loop (common to both pathways) []. There are about 30 enzymes involved in either pathway, where those involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Several of these enzymes are pathway-specific: CbiD, CbiG, and CbiK are specific to the anaerobic route of S. typhimurium, whereas CobE, CobF, CobG, CobN, CobS, CobT, and CobW are unique to the aerobic pathway of P. denitrificans.This entry represents CobM and CibF precorrin-4 C11-methyltransferase (), both as stand-alone enzymes and when CobJ forms part of a bifunctional enzyme. In the aerobic pathway, CobM catalyses the methylation of precorrin-4 at C-11 to yield precorrin-5. The extruded acyl group is then removed in the subsequent step catalysed by CobF. In the anaerobic pathway, CibF catalyses the methylation of cobalt-precorrin-4 to cobalt-precoriin-5 []. Nomenclature note: occasionally precorrin-4 C11-methyltransferase is one of two methyltransferases often referred to as precorrin-3 methylase (the other is precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, ). Short Name:  Cbl_synth_CobM/CibF
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0 Child Features

3 Contains

DB identifier Type Name
IPR014777 Domain Tetrapyrrole methylase, subdomain 1
IPR014776 Domain Tetrapyrrole methylase, subdomain 2
IPR003043 Conserved_site Uroporphiryn-III C-methyltransferase, conserved site

1 Cross References

Identifier
TIGR01465

0 Found In

2 GO Annotations

GO Term Gene Name
GO:0046026 IPR006362
GO:0009236 IPR006362

2 Ontology Annotations

GO Term Gene Name
GO:0046026 IPR006362
GO:0009236 IPR006362

1 Parent Features

DB identifier Type Name
IPR000878 Domain Tetrapyrrole methylase

3 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Brdisv1BdTR11A1048897m.p PAC:35689747 Brachypodium distachyon BdTR11a 299  
Brdisv1BdTR11A1047428m.p PAC:35692794 Brachypodium distachyon BdTR11a 248  
Brdisv1BdTR11A1034287m.p PAC:35676416 Brachypodium distachyon BdTR11a 248  

7 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11215515
            11153269
            12869542
            17163662
            16042605
            12055304
            23922391