Accession | TIGR01140 |
Name | L_thr_O3P_dcar |
Function | threonine-phosphate decarboxylase |
Trusted Cutoff | 290.55 |
Domain Trusted Cutoff | 290.55 |
Noise Cutoff | 276.85 |
Domain Noise Cutoff | 276.85 |
Isology Type | equivalog |
EC Number | 4.1.1.81 |
HMM Length | 331 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Heme, porphyrin, and cobalamin |
Gene Ontology Term | GO:0005737: cytoplasm cellular_component |
| GO:0009236: cobalamin biosynthetic process biological_process |
| GO:0048472: threonine-phosphate decarboxylase activity molecular_function |
Author | Haft DH |
Entry Date | Jan 31 2001 10:10AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This family contains pyridoxal phosphate-binding class II aminotransferases (see PFAM:PF00222) closely related to, yet distinct from, histidinol-phosphate aminotransferase (HisC). It is found in cobalamin biosynthesis operons in Salmonella typhimurium and Bacillus halodurans (each of which also has HisC) and has been shown to have L-threonine-O-3-phosphate decarboxylase activity in Salmonella. Although the gene symbol cobD was assigned in Salmonella, cobD in other contexts refers to a different cobalamin biosynthesis enzyme, modeled by PF03186 and called cbiB in Salmonella. |
References | RN [1]
RM 98112812
RT CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2.
RA Brushaber KR, O'Toole GA, Escalante-Semerena JC
RL J Biol Chem 1998 Jan 30;273(5):2684-91
RN [2]
RM PMID: 12119022
RT Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
RA Cheong CG, Escalante-Semerena JC, Rayment I
RL Biochemistry. 2002 Jul 23;41(29):9079-89. |
Genome Property | GenProp0269: coenzyme B12 biosynthesis from cob(II)yrinate diamide (HMM) |