Anthranilate synthase component II (P00904)

Identification
Name:Anthranilate synthase component II
Synonyms:
  • Glutamine amidotransferase
  • Anthranilate phosphoribosyltransferase
Gene Name:trpD
Enzyme Class:
Biological Properties
General Function:Involved in anthranilate phosphoribosyltransferase activity
Specific Function:Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0L-Glutamine ↔ 1.02-Aminobenzoic acid + 1.0L-Glutamate + 1.0Hydrogen ion + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Aminobenzoic acid + 1.0Phosphoribosyl pyrophosphate → 1.0Pyrophosphate + 1.0N-(5-Phospho-D-ribosyl)anthranilate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0Ammonia ↔ 1.02-Aminobenzoic acid + 1.0Pyruvic acid + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0L-Glutamine ↔ 1.02-Aminobenzoic acid + 1.0Pyruvic acid + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-(5-Phospho-D-ribosyl)anthranilate + 1.0Pyrophosphate ↔ 1.02-Aminobenzoic acid + 1.0Phosphoribosyl pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0L-Glutamine → 1.0Hydrogen ion + 1.02-Aminobenzoic acid + 1.0Pyruvic acid + 1.0L-Glutamate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0L-Glutamic acid+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0L-Glutamine → 1.0L-Glutamic acid + 1.0Pyruvic acid + 1.0Hydrogen ion + 1.02-Aminobenzoic acid + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0 N-(5-phosphoribosyl)-anthranilate+1.0Thumb
1.02-Aminobenzoic acid + 1.0Phosphoribosyl pyrophosphate → 1.0Pyrophosphate + 1.0 N-(5-phosphoribosyl)-anthranilate + 1.0 N-(5-phosphoribosyl)-anthranilate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0L-Glutamine ↔ 1.02-Aminobenzoic acid + 1.0L-Glutamate + 1.0Hydrogen ion + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Aminobenzoic acid + 1.0Phosphoribosyl pyrophosphate → 1.0Pyrophosphate + 1.0N-(5-Phospho-D-ribosyl)anthranilate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Chorismate + 1.0L-Glutamine → 1.0Hydrogen ion + 1.02-Aminobenzoic acid + 1.0Pyruvic acid + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb ← 1.0Thumb+1.0Thumb
1.0N-(5-Phospho-D-ribosyl)anthranilate + 1.0Pyrophosphate ← 1.02-Aminobenzoic acid + 1.0Phosphoribosyl pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-(5-Phospho-D-ribosyl)anthranilate + 1.0Pyrophosphate → 1.02-Aminobenzoic acid + 1.0Phosphoribosyl pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24200 N-(5-phosphoribosyl)-anthranilateMetaboCard
ECMDB011232-Aminobenzoic acidMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB12199ChorismateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB20174N-(5-Phospho-D-ribosyl)anthranilateMetaboCard
ECMDB00280Phosphoribosyl pyrophosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
anthranilate phosphoribosyltransferase activity
anthranilate synthase activity
carbon-carbon lyase activity
catalytic activity
lyase activity
oxo-acid-lyase activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular amino acid metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
glutamine metabolic process
indolalkylamine metabolic process
metabolic process
tryptophan biosynthetic process
tryptophan metabolic process
Gene Properties
Blattner:b1263
Gene OrientationCounterclockwise
Centisome Percentage:28.40
Left Sequence End1317813
Right Sequence End1319408
Gene Sequence:
>1596 bp
ATGGCTGACATTCTGCTGCTCGATAATATCGACTCTTTTACGTACAACCTGGCAGATCAG
TTGCGCAGCAATGGGCATAACGTGGTGATTTACCGCAACCATATTCCGGCGCAAACCTTA
ATTGAACGCCTGGCGACCATGAGCAATCCGGTGCTGATGCTTTCTCCTGGCCCCGGTGTG
CCGAGCGAAGCCGGTTGTATGCCGGAACTCCTCACCCGCTTGCGTGGCAAGCTGCCCATT
ATTGGCATTTGCCTCGGACATCAGGCGATTGTCGAAGCTTACGGGGGCTATGTCGGTCAG
GCGGGCGAAATTCTCCACGGTAAAGCCTCCAGCATTGAACATGACGGTCAGGCGATGTTT
GCCGGATTAACAAACCCGCTGCCGGTGGCGCGTTATCACTCGCTGGTTGGCAGTAACATT
CCGGCCGGTTTAACCATCAACGCCCATTTTAATGGCATGGTGATGGCAGTACGTCACGAT
GCGGATCGCGTTTGTGGATTCCAGTTCCATCCGGAATCCATTCTCACCACCCAGGGCGCT
CGCCTGCTGGAACAAACGCTGGCCTGGGCGCAGCAGAAACTAGAGCCAGCCAACACGCTG
CAACCGATTCTGGAAAAACTGTATCAGGCGCAGACGCTTAGCCAACAAGAAAGCCACCAG
CTGTTTTCAGCGGTGGTGCGTGGCGAGCTGAAGCCGGAACAACTGGCGGCGGCGCTGGTG
AGCATGAAAATTCGCGGTGAGCACCCGAACGAGATCGCCGGGGCAGCAACCGCGCTACTG
GAAAACGCAGCGCCGTTCCCGCGCCCGGATTATCTGTTTGCTGATATCGTCGGTACTGGC
GGTGACGGCAGCAACAGTATCAATATTTCTACCGCCAGTGCGTTTGTCGCCGCGGCCTGT
GGGCTGAAAGTGGCGAAACACGGCAACCGTAGCGTCTCCAGTAAATCTGGTTCGTCCGAT
CTGCTGGCGGCGTTCGGTATTAATCTTGATATGAACGCCGATAAATCGCGCCAGGCGCTG
GATGAGTTAGGTGTATGTTTCCTCTTTGCGCCGAAGTATCACACCGGATTCCGCCACGCG
ATGCCGGTTCGCCAGCAACTGAAAACCCGCACCCTGTTCAATGTGCTGGGGCCATTGATT
AACCCGGCGCATCCGCCGCTGGCGTTAATTGGTGTTTATAGTCCGGAACTGGTGCTGCCG
ATTGCCGAAACCTTGCGCGTGCTGGGGTATCAACGCGCGGCGGTGGTGCACAGCGGCGGG
ATGGATGAAGTTTCATTACACGCGCCGACAATCGTTGCCGAACTGCATGACGGCGAAATT
AAAAGCTATCAGCTCACCGCAGAAGACTTTGGCCTGACACCCTACCACCAGGAGCAACTG
GCAGGCGGAACACCGGAAGAAAACCGTGACATTTTAACACGTTTGTTACAAGGTAAAGGC
GACGCCGCCCATGAAGCAGCCGTCGCTGCGAACGTCGCCATGTTAATGCGCCTGCATGGC
CATGAAGATCTGCAAGCCAATGCGCAAACCGTTCTTGAGGTACTGCGCAGTGGTTCCGCT
TACGACAGAGTCACCGCACTGGCGGCACGAGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:531
Protein Molecular Weight:56869
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Anthranilate synthase component II
MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGV
PSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMF
AGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGA
RLLEQTLAWAQQKLEPANTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV
SMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAAC
GLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHA
MPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGG
MDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKG
DAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG
References
External Links:
ResourceLink
Uniprot ID:P00904
Uniprot Name:TRPG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742056
Ecogene ID:EG11027
Ecocyc:EG11027
ColiBase:b1263
Kegg Gene:b1263
EchoBASE ID:EB1020
CCDB:TRPG_ECOLI
BacMap:16129224
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
  • Horowitz, H., Christie, G. E., Platt, T. (1982). "Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli." J Mol Biol 156:245-256. Pubmed: 6283099
  • Li, S. L., Hanlon, J., Yanofsky, C. (1974). "Structural homology of the glutamine amidotransferase subunits of the anthranilate synthetases of Escherichia coli, Salmonella typhimurium and Serratia marcescens." Nature 248:48-50. Pubmed: 4594441
  • 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