Tryptophan biosynthesis protein trpCF (P00909)

Identification
Name:Tryptophan biosynthesis protein trpCF
Synonyms:
  • Indole-3-glycerol phosphate synthase
  • IGPS
  • N-(5'-phospho-ribosyl)anthranilate isomerase
  • PRAI
Gene Name:trpC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the trpF domain; the second reaction is catalyzed by the synthase, coded by the trpC domain
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate + 1.0Hydrogen ion ↔ 1.0Indoleglycerol phosphate + 1.0Carbon dioxide + 1.0Water
ReactionCard
1.0Thumb → 1.0Thumb
1.0N-(5-Phospho-D-ribosyl)anthranilate → 1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate ↔ 1.0Indoleglycerol phosphate + 1.0Carbon dioxide + 1.0Water
ReactionCard
1.0Thumb ↔ 1.0Thumb
1.0N-(5-Phospho-D-ribosyl)anthranilate ↔ 1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate
ReactionCard
SMPDB Reactions:
1.0 N-(5-phosphoribosyl)-anthranilate+1.0Thumb → 1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate+1.0Thumb
1.0 N-(5-phosphoribosyl)-anthranilate + 1.0 N-(5-phosphoribosyl)-anthranilate → 1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate + 1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate
ReactionCard
1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate + 1.0Hydrogen ion + 1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate → 1.0Water + 1.0Carbon dioxide
ReactionCard
1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate+1.0Thumb
1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate + 1.0Hydrogen ion + 1.01-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphate → 1.0Water + 1.0Carbon dioxide + 1.0(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + 1.0(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
ReactionCard
1.0 N-(5-phosphoribosyl)-anthranilate+1.0Thumb → 1.0Thumb
1.0 N-(5-phosphoribosyl)-anthranilate + 1.0 N-(5-phosphoribosyl)-anthranilate → 1.01-(2-Carboxyphenylamino)-1'-deoxyribulose-5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate+1.0Thumb
1.01-(2-Carboxyphenylamino)-1'-deoxyribulose-5'-phosphate + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.0Water + 1.0(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + 1.0(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate + 1.0Hydrogen ion ↔ 1.0Indoleglycerol phosphate + 1.0Carbon dioxide + 1.0Water
ReactionCard
1.0Thumb → 1.0Thumb
1.0N-(5-Phospho-D-ribosyl)anthranilate → 1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.01-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate → 1.0Indoleglycerol phosphate + 1.0Carbon dioxide + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24200 N-(5-phosphoribosyl)-anthranilateMetaboCard
ECMDB24202(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphateMetaboCard
ECMDB200191-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphateMetaboCard
ECMDB214671-(2-Carboxyphenylamino)-1'-deoxyribulose-5'-phosphateMetaboCard
ECMDB242011-(o-carboxyphenylamino)-1'-deoxyribulose 5'-phosphateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB20160Indoleglycerol phosphateMetaboCard
ECMDB20174N-(5-Phospho-D-ribosyl)anthranilateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
indole-3-glycerol-phosphate synthase activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
isomerase activity
lyase activity
phosphoribosylanthranilate isomerase activity
Process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
indolalkylamine metabolic process
metabolic process
tryptophan metabolic process
Gene Properties
Blattner:b1262
Gene OrientationCounterclockwise
Centisome Percentage:28.37
Left Sequence End1316451
Right Sequence End1317809
Gene Sequence:
>1359 bp
ATGATTAGCGTAACCCTTAGCCAACTTACCGACATTCTCAACGGTGAACTGCAAGGTGCA
GATATCACCCTTGATGCTGTAACCACTGATACCCGAAAACTGACGCCGGGCTGCCTGTTT
GTTGCCCTGAAAGGCGAACGTTTTGATGCCCACGATTTTGCCGACCAGGCGAAAGCTGGC
GGCGCAGGCGCACTACTGGTTAGCCGTCCGCTGGACATCGACCTGCCGCAGTTAATCGTC
AAGGATACGCGTCTGGCGTTTGGTGAACTGGCTGCATGGGTTCGCCAGCAAGTTCCGGCG
CGCGTGGTTGCTCTGACGGGGTCCTCCGGCAAAACCTCCGTTAAAGAGATGACGGCGGCG
ATTTTAAGCCAGTGCGGCAACACGCTTTATACGGCAGGCAATCTCAACAACGACATCGGT
GTACCGATGACGCTGTTGCGCTTAACGCCGGAATACGATTACGCAGTTATTGAACTTGGC
GCGAACCATCAGGGCGAAATAGCCTGGACTGTGAGTCTGACTCGCCCGGAAGCTGCGCTG
GTCAACAACCTGGCAGCGGCGCATCTGGAAGGTTTTGGCTCGCTTGCGGGTGTCGCGAAA
GCGAAAGGTGAAATCTTTAGCGGCCTGCCGGAAAACGGTATCGCCATTATGAACGCCGAC
AACAACGACTGGCTGAACTGGCAGAGCGTAATTGGCTCACGCAAAGTGTGGCGTTTCTCA
CCCAATGCCGCCAACAGCGATTTCACCGCCACCAATATCCATGTGACCTCGCACGGTACG
GAATTTACCCTACAAACCCCAACCGGTAGCGTCGATGTTCTGCTGCCGTTGCCGGGGCGT
CACAATATTGCGAATGCGCTGGCAGCCGCTGCGCTCTCCATGTCCGTGGGCGCAACGCTT
GATGCTATCAAAGCGGGGCTGGCAAATCTGAAAGCTGTTCCAGGCCGTCTGTTCCCCATC
CAACTGGCAGAAAACCAGTTGCTGCTCGACGACTCCTACAACGCCAATGTCGGTTCAATG
ACTGCAGCAGTCCAGGTACTGGCTGAAATGCCGGGCTACCGCGTGCTGGTGGTGGGCGAT
ATGGCGGAACTGGGCGCTGAAAGCGAAGCCTGCCATGTACAGGTGGGCGAGGCGGCAAAA
GCTGCTGGTATTGACCGCGTGTTAAGCGTGGGTAAACAAAGCCATGCTATCAGCACCGCC
AGCGGCGTTGGCGAACATTTTGCTGATAAAACTGCGTTAATTACGCGTCTTAAATTACTG
ATTGCTGAGCAACAGGTAATTACGATTTTAGTTAAGGGTTCACGTAGTGCCGCCATGGAA
GAGGTAGTACGCGCTTTACAGGAGAATGGGACATGTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:452
Protein Molecular Weight:49361
Protein Theoretical pI:6
PDB File:1PII
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Tryptophan biosynthesis protein trpCF
MQTVLAKIVADKAIWVEARKQQQPLASFQNEVQPSTRHFYDALQGARTAFILECKKASPS
KGVIRDDFDPARIAAIYKHYASAISVLTDEKYFQGSFNFLPIVSQIAPQPILCKDFIIDP
YQIYLARYYQADACLLMLSVLDDDQYRQLAAVAHSLEMGVLTEVSNEEEQERAIALGAKV
VGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSALM
AHDDLHAAVRRVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVM
AAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGNEEQLYIDTLREALPAHVAIWKALS
VGETLPAREFQHVDKYVLDNGQGGSGQRFDWSLLNGQSLGNVLLAGGLGADNCVEAAQTG
CAGLDFNSAVESQPGIKDARLLASVFQTLRAY
References
External Links:
ResourceLink
Uniprot ID:P00909
Uniprot Name:TRPC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674322
PDB ID:1PII
Ecogene ID:EG11026
Ecocyc:EG11026
ColiBase:b1262
Kegg Gene:b1262
EchoBASE ID:EB1019
CCDB:TRPC_ECOLI
BacMap:90111239
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
  • Christie, G. E., Platt, T. (1980). "Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions." J Mol Biol 142:519-530. Pubmed: 7007653
  • 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
  • Horowitz, H., Van Arsdell, J., Platt, T. (1983). "Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium." J Mol Biol 169:775-797. Pubmed: 6355484
  • Milkman, R., Bridges, M. M. (1993). "Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons." Genetics 133:455-468. Pubmed: 8095913
  • Wilmanns, M., Priestle, J. P., Niermann, T., Jansonius, J. N. (1992). "Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution." J Mol Biol 223:477-507. Pubmed: 1738159
  • Wilmanns, M., Schlagenhauf, E., Fol, B., Jansonius, J. N. (1990). "Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue." Protein Eng 3:173-180. Pubmed: 2184433
  • Yanofsky, C., Platt, T., Crawford, I. P., Nichols, B. P., Christie, G. E., Horowitz, H., VanCleemput, M., Wu, A. M. (1981). "The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Nucleic Acids Res 9:6647-6668. Pubmed: 7038627