Bifunctional purine biosynthesis protein purH (P15639)

Identification
Name:Bifunctional purine biosynthesis protein purH
Synonyms:
  • Phosphoribosylaminoimidazolecarboxamide formyltransferase
  • AICAR transformylase
  • IMP cyclohydrolase
  • ATIC
  • IMP synthase
  • Inosinicase
Gene Name:purH
Enzyme Class:
Biological Properties
General Function:Involved in IMP cyclohydrolase activity
Specific Function:10-formyltetrahydrofolate + 5-amino-1-(5- phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Cellular Location:Cytoplasmic
SMPDB Pathways:
  • One Carbon Pool by Folate I PW001735
  • One carbon pool by folate PW000773
  • 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
1.0Water + 1.0Inosinic acid ↔ 1.0Phosphoribosyl formamidocarboxamide
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0AICAR ↔ 1.0Tetrahydrofolic acid + 1.0Phosphoribosyl formamidocarboxamide
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0AICAR → 1.0Tetrahydrofolic acid + 1.0Phosphoribosyl formamidocarboxamide
ReactionCard
SMPDB Reactions:
1.0Tetrahydrofolic acid+1.0Thumb+1.0Thumb → 1.010-Formyltetrahydrofolate+1.0Thumb+1.0Thumb
1.0Tetrahydrofolic acid + 1.0FAICAR + 1.0Tetrahydrofolic acid → 1.010-Formyltetrahydrofolate + 1.0AICAR + 1.0N10-Formyl-THF
ReactionCard
1.0Thumb+1.010-Formyltetrahydrofolate+1.0Thumb → 1.0Thumb+1.0Thumb
1.0AICAR + 1.010-Formyltetrahydrofolate + 1.0N10-Formyl-THF → 1.0FAICAR + 1.0tetrahydropteroyl mono-L-glutamate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0FAICAR ↔ 1.0Inosinic acid + 1.0Water
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb
1.0Water + 1.0Inosinic acid ↔ 1.0Phosphoribosyl formamidocarboxamide
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0AICAR → 1.0Tetrahydrofolic acid + 1.0Phosphoribosyl formamidocarboxamide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Phosphoribosyl formamidocarboxamide ↔ 1.0Phosphoribosyl formamidocarboxamide + 1.0Tetrahydrofolic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb
1.0Inosinic acid + 1.0Water → 1.0Phosphoribosyl formamidocarboxamide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01517AICARMetaboCard
ECMDB24188FAICARMetaboCard
ECMDB04085Inosinic acidMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB01439Phosphoribosyl formamidocarboxamideMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB24261tetrahydropteroyl mono-L-glutamateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
cyclohydrolase activity
glycine hydroxymethyltransferase activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
hydroxymethyl-, formyl- and related transferase activity
IMP cyclohydrolase activity
methyltransferase activity
phosphoribosylaminoimidazolecarboxamide formyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
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:b4006
Gene OrientationCounterclockwise
Centisome Percentage:90.61
Left Sequence End4203966
Right Sequence End4205555
Gene Sequence:
>1590 bp
ATGACGCAAACTCTGTTAGCGATTGAAAATTTGTCGGTGGGTTTTCGCCATCAGCAAACC
GTACGTACAGTAGTCAATGATGTTTCACTACAGATTGAGGCTGGCGAAACGCTGGCGCTG
GTGGGTGAGTCAGGTTCAGGCAAAAGCGTTACCGCGCTGTCAATTTTACGCCTGCTCCCT
TCCCCGCCGGTTGAATATCTCTCCGGCGATATTCGTTTTCATGGCGAATCGCTGCTTCAC
GCCAGCGATCAAACGTTGCGCGGTGTACGCGGTAATAAGATCGCCATGATTTTTCAGGAA
CCGATGGTGTCGTTAAATCCATTGCATACCCTGGAAAAACAGCTTTATGAAGTGCTTTCA
CTCCACCGCGGGATGCGTCGGGAAGCGGCTCGTGGCGAAATTCTTAACTGCCTTGATCGC
GTTGGTATCCGCCAGGCGGCAAAACGGCTGACAGATTATCCGCATCAGCTCTCCGGCGGC
GAACGGCAGCGGGTGATGATTGCGATGGCGCTGTTAACGCGACCGGAATTATTAATTGCC
GATGAACCGACCACCGCACTGGACGTCTCTGTCCAGGCGCAGATTTTACAGCTGTTGCGC
GAACTGCAAGGCGAGCTGAATATGGGCATGCTGTTTATTACTCATAACCTCAGCATTGTC
AGAAAACTGGCCCACCGCGTGGCGGTAATGCAAAACGGTCGCTGTGTCGAGCAAAATTAC
GCCGCTACGCTATTTGCATCACCCACTCATCCTTACACACAAAAGCTACTCAACAGTGAA
CCGTCAGGCGATCCAGTGCCGTTGCCAGAACCTGCCTCAACGTTGCTGGATGTTGAACAG
CTTCAGGTTGCCTTCCCCATTCGCAAAGGGATTTTGAAGCGCATTGTGGATCATAATGTG
GTGGTGAAAAACATCAGTTTTACGCTACGAGCGGGTGAAACACTGGGTTTAGTGGGCGAG
TCCGGTTCCGGGAAAAGTACGACGGGACTGGCGCTGCTGCGACTGATTAATTCTCAGGGC
AGCATCATCTTTGACGGTCAGCCACTGCAAAATTTAAATCGCCGCCAGCTGTTACCTATT
CGTCATCGCATTCAGGTGGTATTTCAGGATCCAAACTCCTCGCTCAACCCACGACTCAAC
GTTTTGCAGATTATTGAGGAAGGCTTACGGGTTCACCAGCCGACGCTTTCTGCCGCACAA
CGCGAACAACAAGTGATAGCCGTGATGCATGAAGTGGGATTAGATCCTGAAACACGCCAC
CGTTATCCGGCGGAGTTCTCTGGTGGTCAGCGACAACGTATTGCGATTGCCAGGGCATTA
ATTCTTAAGCCCTCGCTGATCATACTTGATGAACCGACATCATCACTCGACAAAACGGTA
CAGGCGCAAATATTGACGCTATTGAAATCATTGCAACAAAAGCATCAACTGGCCTATTTG
TTTATCAGCCACGATTTGCACGTTGTCCGCGCGTTATGTCATCAGGTTATCATACTGCGA
CAAGGGGAAGTAGTGGAACAAGGACCGTGCGCGCGCGTGTTTGCCACACCGCAGCAGGAG
TATACGCGTCAGCTACTGGCGTTGAGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:529
Protein Molecular Weight:57329
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional purine biosynthesis protein purH
MQQRRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGF
PEMMDGRVKTLHPKVHGGILGRRGQDDAIMEEHQIQPIDMVVVNLYPFAQTVAREGCSLE
DAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDNEGSLTLATRFDLAIKAF
EHTAAYDSMIANYFGSMVPAYHGESKEAAGRFPRTLNLNFIKKLDMRYGENSHQQAAFYI
EENVKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSI
LDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAIISRQFVEVIIAPSASEEALKITAAKQ
NVRVLTCGQWGERVPGLDFKRVNGGLLVQDRDLGMVGAEELRVVTKRQPSEQELRDALFC
WKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADEGLEVKGSSMASDAFFP
FRDGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRHFRH
References
External Links:
ResourceLink
Uniprot ID:P15639
Uniprot Name:PUR9_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675289
Ecogene ID:EG10795
Ecocyc:EG10795
ColiBase:b4006
Kegg Gene:b4006
EchoBASE ID:EB0788
CCDB:PUR9_ECOLI
BacMap:16131836
General Reference:
  • Aiba, A., Mizobuchi, K. (1989). "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli." J Biol Chem 264:21239-21246. Pubmed: 2687276
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • 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
  • Flannigan, K. A., Hennigan, S. H., Vogelbacker, H. H., Gots, J. S., Smith, J. M. (1990). "Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus." Mol Microbiol 4:381-392. Pubmed: 2192230
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842