Alpha-ribazole phosphatase (P52086)

Identification
Name:Alpha-ribazole phosphatase
Synonyms:
  • Alpha-ribazole-5'-phosphate phosphatase
Gene Name:cobC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Converts N1-(5-phospho-alpha-D-ribosyl)-5,6- dimethylbenzimidazole into N1-alpha-D-ribosyl-5,6- dimethylbenzimidazole; involved in the assembly of the nucleotide loop of cobalamin
Cellular Location:Cytoplasmic
SMPDB Pathways:
  • adenosylcobalamin salvage from cobinamide PW001884
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N1-(5-Phospho-a-D-ribosyl)-5,6-dimethylbenzimidazole + 1.0Water → 1.0Phosphate + 1.0N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazole
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N1-(5-Phospho-a-D-ribosyl)-5,6-dimethylbenzimidazole + 1.0Water ↔ 1.0N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazole + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0coenzyme B12
1.0Adenosylcobalamin 5'-phosphate + 1.0Water → 1.0Phosphate + 1.0coenzyme B12
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N1-(5-Phospho-a-D-ribosyl)-5,6-dimethylbenzimidazole + 1.0Water → 1.0Phosphate + 1.0N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazole
ReactionCard
1.0adenosylcobalamin 5'-phosphate+1.0Thumb → 1.0Thumb+1.0Thumb
1.0adenosylcobalamin 5'-phosphate + 1.0Water → 1.0Adenosylcobalamin + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosylcobalamin + 1.0Water → 1.0Adenosylcobalamin + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB02086AdenosylcobalaminMetaboCard
ECMDB23095Adenosylcobalamin 5'-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB03882N1-(5-Phospho-a-D-ribosyl)-5,6-dimethylbenzimidazoleMetaboCard
ECMDB11112N1-(alpha-D-ribosyl)-5,6-dimethyl-benzimidazoleMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
alpha-ribazole phosphatase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphatase activity
phosphoric ester hydrolase activity
Process
cobalamin biosynthetic process
metabolic process
nitrogen compound metabolic process
porphyrin biosynthetic process
porphyrin metabolic process
tetrapyrrole metabolic process
Gene Properties
Blattner:b0638
Gene OrientationCounterclockwise
Centisome Percentage:14.41
Left Sequence End668519
Right Sequence End669130
Gene Sequence:
>612 bp
ATGCGACTGTGGTTAATTCGTCATGGTGAAACGCAAGCGAATATCGATGGTCTTTACAGC
GGTCATGCGCCCACCCCCCTGACCGCGCGCGGTATTGAGCAAGCGCAAAATCTGCATACG
CTGCTACATGGTGTTTCCTTTGATCTGGTTTTATGCAGTGAACTGGAACGGGCACAGCAT
ACCGCGCGACTGGTTCTCAGTGACCGCCAGCTCCCCGTGCAAATCATACCTGAACTCAAC
GAAATGTTTTTTGGCGACTGGGAGATGCGACATCATCGCGACCTCATGCAAGAAGATGCC
GAAAACTATAGCGCGTGGTGCAATGACTGGCAGCATGCAATCCCCACGAACGGTGAAGGA
TTTCAGGCATTTTCGCAACGTGTGGAACGCTTTATCGCAAGGCTTAGTGAATTTCAGCAC
TATCAGAATATTTTAGTCGTCAGCCATCAGGGTGTACTGAGTCTGTTAATCGCCCGTTTA
ATTGGCATGCCTGCCGAAGCTATGTGGCATTTTCGCGTTGACCAGGGGTGTTGGAGCGCC
ATTGATATCAACCAAAAATTCGCGACGCTACGCGTCCTCAATAGCCGTGCCATCGGGGTC
GAGAATGCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:203
Protein Molecular Weight:23308
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Alpha-ribazole phosphatase
MRLWLIRHGETQANIDGLYSGHAPTPLTARGIEQAQNLHTLLHGVSFDLVLCSELERAQH
TARLVLSDRQLPVQIIPELNEMFFGDWEMRHHRDLMQEDAENYSAWCNDWQHAIPTNGEG
FQAFSQRVERFIARLSEFQHYQNILVVSHQGVLSLLIARLIGMPAEAMWHFRVDQGCWSA
IDINQKFATLRVLNSRAIGVENA
References
External Links:
ResourceLink
Uniprot ID:P52086
Uniprot Name:COBC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062256
Ecogene ID:EG13240
Ecocyc:EG13240
ColiBase:b0638
Kegg Gene:b0638
EchoBASE ID:EB3029
CCDB:COBC_ECOLI
BacMap:16128621
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232