Phosphoribosylaminoimidazole carboxylase ATPase subunit (P09029)

Identification
Name:Phosphoribosylaminoimidazole carboxylase ATPase subunit
Synonyms:
  • AIR carboxylase
  • AIRC
Gene Name:purK
Enzyme Class:
Biological Properties
General Function:Involved in phosphoribosylaminoimidazole carboxylase activity
Specific Function:Possesses an ATPase activity that is dependent on the presence of AIR (aminoimidazole ribonucleotide). The association of purK and purE produces an enzyme complex capable of converting AIR to CAIR efficiently under physiological condition
Cellular Location:Not Available
SMPDB Pathways:
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.05-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole+1.0Thumb
1.0Adenosine triphosphate + 1.05-Aminoimidazole ribonucleotide + 1.0Hydrogen carbonate ↔ 1.0ADP + 1.0Phosphate + 1.05-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole + 1.05-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate ↔ 1.05-Aminoimidazole ribonucleotide + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0N5-Carboxyaminoimidazole ribonucleotide+1.0Adenosine diphosphate+1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.05-Aminoimidazole ribonucleotide + 1.0Hydrogen carbonate + 1.0Adenosine triphosphate → 1.0N5-Carboxyaminoimidazole ribonucleotide + 1.0Adenosine diphosphate + 1.0Phosphate + 2.0Hydrogen ion + 1.0N5-Carboxyaminoimidazole ribonucleotide + 1.0ADP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.05-Aminoimidazole ribonucleotide + 1.0Adenosine triphosphate + 1.0Hydrogen carbonate → 1.05-Phosphoribosyl-5-carboxyaminoimidazole + 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Aminoimidazole ribonucleotide + 1.0Carbonic acid → 1.0ADP + 1.0Inorganic phosphate + 1.05-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB012355-Aminoimidazole ribonucleotideMetaboCard
ECMDB230205-carboxyamino-1-(5-phospho-D-ribosyl)imidazoleMetaboCard
ECMDB211785-Phosphoribosyl-5-carboxyaminoimidazoleMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01317N5-Carboxyaminoimidazole ribonucleotideMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
nucleoside binding
phosphoribosylaminoimidazole carboxylase activity
purine nucleoside binding
Process
'de novo' IMP biosynthetic process
cellular nitrogen compound metabolic process
IMP biosynthetic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside monophosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside monophosphate biosynthetic process
Gene Properties
Blattner:b0522
Gene OrientationCounterclockwise
Centisome Percentage:11.87
Left Sequence End550750
Right Sequence End551817
Gene Sequence:
>1068 bp
ATGAGTGGTCAAGGAAAGCGATTAATGGTGATGGCAGGCGGAACCGGTGGACATGTATTC
CCGGGACTGGCGGTTGCGCACCATCTAATGGCTCAGGGTTGGCAAGTTCGCTGGCTGGGG
ACTGCCGACCGTATGGAAGCGGACTTAGTGCCAAAACATGGCATCGAAATTGATTTCATT
CGTATCTCTGGTCTGCGTGGAAAAGGTATAAAAGCACTGATAGCTGCCCCGCTGCGTATC
TTCAACGCCTGGCGTCAGGCGCGGGCGATTATGAAAGCGTACAAACCTGACGTGGTGCTC
GGTATGGGAGGCTACGTGTCAGGTCCAGGTGGTCTGGCCGCGTGGTCGTTAGGCATTCCG
GTTGTACTTCATGAACAAAACGGTATTGCGGGCTTAACCAATAAATGGCTGGCGAAGATT
GCCACCAAAGTGATGCAGGCGTTTCCAGGTGCTTTCCCTAATGCGGAAGTAGTGGGTAAC
CCGGTGCGTACCGATGTGTTGGCGCTGCCGTTGCCGCAGCAACGTTTGGCTGGACGTGAA
GGTCCGGTTCGTGTGCTGGTAGTGGGTGGTTCTCAGGGCGCACGCATTCTTAACCAGACA
ATGCCGCAGGTTGCTGCGAAACTGGGTGATTCAGTCACTATCTGGCATCAGAGCGGCAAA
GGTTCGCAACAATCCGTTGAACAGGCGTATGCCGAAGCGGGGCAACCGCAGCATAAAGTG
ACGGAATTTATTGATGATATGGCGGCGGCGTATGCGTGGGCGGATGTCGTCGTTTGCCGC
TCCGGTGCGTTAACGGTGAGTGAAATCGCCGCGGCAGGACTACCGGCGTTGTTTGTGCCG
TTTCAACATAAAGACCGCCAGCAATACTGGAATGCGCTACCGCTGGAAAAAGCGGGCGCA
GCCAAAATTATCGAGCAGCCACAGCTTAGCGTGGATGCTGTCGCCAACACCCTGGCCGGG
TGGTCGCGAGAAACCTTATTAACCATGGCAGAACGCGCCCGCGCTGCATCCATTCCGGAT
GCCACCGAGCGAGTGGCAAATGAAGTGAGCCGGGTTGCCCGGGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:355
Protein Molecular Weight:39461
Protein Theoretical pI:6
PDB File:1B6S
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylaminoimidazole carboxylase ATPase subunit
MKQVCVLGNGQLGRMLRQAGEPLGIAVWPVGLDAEPAAVPFQQSVITAEIERWPETALTR
ELARHPAFVNRDVFPIIADRLTQKQLFDKLHLPTAPWQLLAERSEWPAVFDRLGELAIVK
RRTGGYDGRGQWRLRANETEQLPAECYGECIVEQGINFSGEVSLVGARGFDGSTVFYPLT
HNLHQDGILRTSVAFPQANAQQQAQAEEMLSAIMQELGYVGVMAMECFVTPQGLLINELA
PRVHNSGHWTQNGASISQFELHLRAITDLPLPQPVVNNPSVMINLIGSDVNYDWLKLPLV
HLHWYDKEVRPGRKVGHLNLTDSDTSRLTATLEALIPLLPPEYASGVIWAQSKFG
References
External Links:
ResourceLink
Uniprot ID:P09029
Uniprot Name:PURK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321971
PDB ID:1B6S
Ecogene ID:EG10796
Ecocyc:EG10796
ColiBase:b0522
Kegg Gene:b0522
EchoBASE ID:EB0789
CCDB:PURK_ECOLI
BacMap:16128506
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
  • Meyer, E., Leonard, N. J., Bhat, B., Stubbe, J., Smith, J. M. (1992). "Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway." Biochemistry 31:5022-5032. Pubmed: 1534690
  • Thoden, J. B., Kappock, T. J., Stubbe, J., Holden, H. M. (1999). "Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily." Biochemistry 38:15480-15492. Pubmed: 10569930
  • Tiedeman, A. A., Keyhani, J., Kamholz, J., Daum, H. A. 3rd, Gots, J. S., Smith, J. M. (1989). "Nucleotide sequence analysis of the purEK operon encoding 5'-phosphoribosyl-5-aminoimidazole carboxylase of Escherichia coli K-12." J Bacteriol 171:205-212. Pubmed: 2464576
  • Watanabe, W., Sampei, G., Aiba, A., Mizobuchi, K. (1989). "Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis." J Bacteriol 171:198-204. Pubmed: 2644189