Identification
Name:Cob(I)yrinic acid a,c-diamide adenosyltransferase
Synonyms:
  • Cob(I)alamin adenosyltransferase
  • Corrinoid adenosyltransferase
Gene Name:btuR
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids
Cellular Location:Cytoplasm
SMPDB Pathways:
  • adenosylcobalamin salvage from cobinamide PW001884
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Adenosyl cobyrinate a,c diamide+1.0Thumb
1.0Cob(I)yrinate a,c diamide + 1.0Adenosine triphosphate ↔ 1.0Adenosyl cobyrinate a,c diamide + 1.0Triphosphate
ReactionCard
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Cobinamide+1.0Thumb+1.0Thumb1.0Adenosyl cobinamide+1.0Triphosphate+1.0Thumb+1.0Thumb
1.0Cobinamide + 1.0Adenosine triphosphate + 1.0Cobinamide → 1.0Adenosyl cobinamide + 1.0Triphosphate + 1.0Adenosyl cobinamide + 1.0Triphosphate
ReactionCard
1.0Cobalamin+1.0Thumb+1.0Thumb1.0coenzyme B12+1.0Thumb+1.0Thumb
1.0Cobalamin + 1.0Adenosine triphosphate + 1.0vitamin B12 → 1.0coenzyme B12 + 1.0Triphosphate + 1.0Polyphosphate
ReactionCard
1.0Thumb+1.0Cobalamin+1.0Thumb1.0Triphosphate+1.0Adenosylcobalamin+1.0Thumb
1.0Adenosine triphosphate + 1.0Cobalamin + 1.0vitamin B12 → 1.0Triphosphate + 1.0Adenosylcobalamin + 1.0Triphosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB06903Adenosyl cobinamideMetaboCard
ECMDB23739Adenosyl cobyrinate a,c diamideMetaboCard
ECMDB23132Adenosylcob(III)yrinic acid a,c-diamideMetaboCard
ECMDB02086AdenosylcobalaminMetaboCard
ECMDB04040Cob(I)alaminMetaboCard
ECMDB01083Cob(I)yrinate a,c diamideMetaboCard
ECMDB06902CobinamideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB23829PolyphosphateMetaboCard
ECMDB03379TriphosphateMetaboCard
ECMDB23097vitamin B12MetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
cob(I)yrinic acid a,c-diamide adenosyltransferase activity
nucleoside binding
purine nucleoside binding
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
cobalamin biosynthetic process
metabolic process
nitrogen compound metabolic process
porphyrin biosynthetic process
porphyrin metabolic process
tetrapyrrole metabolic process
Gene Properties
Blattner:b1270
Gene OrientationCounterclockwise
Centisome Percentage:28.58
Left Sequence End1325791
Right Sequence End1326381
Gene Sequence:
>591 bp
ATGCAGTCTGAACGTATTTATTTGGTATGGGCCCATCCTCGTCATGATTCATTGACCGCA
CATATTGCTGATGCGATCCATCAGCGGGCAATGGAGCGGAAAATACAGGTGACGGAACTC
GATTTATATCGGCGTAATTTCAACCCAGTGATGACGCCGGAAGATGAACCAGACTGGAAG
AATATGGATAAACGTTATTCTCCAGAGGTTCATCAGCTTTATTCAGAGCTGCTTGAACAT
GACACGTTAGTGGTGGTTTTTCCTCTCTGGTGGTACAGCTTCCCGGCAATGCTAAAAGGA
TATATTGACAGAGTATGGAATAATGGGCTGGCTTATGGAGATGGGCACAAATTACCATTC
AATAAAGTTCGTTGGGTGGCGCTGGTTGGAGGAGACAAAGAATCATTTGTCCAGATGGGC
TGGGAAAAAAATATAAGCGATTATTTAAAAAATATGTGCAGTTATCTTGGTATTGAAGAT
GCCGATGTCACTTTCTTGTGTAATACAGTGGTATTCGATGGGGAAGAACTTCACGCGAGC
TATTATCAGTCGTTATTATCTCAGGTACGGGATATGGTAGATGCACTATAA
Protein Properties
Pfam Domain Function:
Protein Residues:196
Protein Molecular Weight:21999
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cob(I)yrinic acid a,c-diamide adenosyltransferase
MSDERYQQRQQRVKEKVDARVAQAQDERGIIIVFTGNGKGKTTAAFGTATRAVGHGKKVG
VVQFIKGTWPNGERNLLEPHGVEFQVMATGFTWDTQNRESDTAACREVWQHAKRMLADSS
LDMVLLDELTYMVAYDYLPLEEVVQALNERPHQQTVIITGRGCHRDILELADTVSELRPV
KHAFDAGVKAQIGIDY
References
External Links:
ResourceLink
Uniprot ID:P0A9H5
Uniprot Name:BTUR_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062477
Ecogene ID:EG10130
Ecocyc:EG10130
ColiBase:b1270
Kegg Gene:b1270
EchoBASE ID:EB0128
CCDB:BTUR_ECOLI
BacMap:16129231
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Lundrigan, M. D., Kadner, R. J. (1989). "Altered cobalamin metabolism in Escherichia coli btuR mutants affects btuB gene regulation." J Bacteriol 171:154-161. Pubmed: 2644187