Tryptophan biosynthesis protein TrpCF

Details

Name
Tryptophan biosynthesis protein TrpCF
Synonyms
  • trpF
Gene Name
trpC
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016472|Tryptophan biosynthesis protein TrpCF
MMQTVLAKIVADKAIWVEARKQQQPLASFQNEVQPSTRHFYDALQGARTAFILECKKASP
SKGVIRDDFDPARIAAIYKHYASAISVLTDEKYFQGSFNFLPIVSQIAPQPILCKDFIID
PYQIYLARYYQADACLLMLSVLDDDQYRQLAAVAHSLEMGVLTEVSNEEEQERAIALGAK
VVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSAL
MAHDDLHAAVRRVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEV
MAAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGNEEQLYIDTLREALPAHVAIWKAL
SVGETLPAREFQHVDKYVLDNGQGGSGQRFDWSLLNGQSLGNVLLAGGLGADNCVEAAQT
GCAGLDFNSAVESQPGIKDARLLASVFQTLRAY
Number of residues
453
Molecular Weight
49491.84
Theoretical pI
5.61
GO Classification
Functions
indole-3-glycerol-phosphate synthase activity / phosphoribosylanthranilate isomerase activity
Processes
tryptophan biosynthetic process
General Function
Phosphoribosylanthranilate isomerase 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016473|Tryptophan biosynthesis protein TrpCF (trpC)
ATGCAAACCGTTTTAGCGAAAATCGTCGCAGACAAGGCGATTTGGGTAGAAGCCCGCAAA
CAGCAGCAACCGCTGGCCAGTTTTCAGAATGAGGTTCAGCCGAGCACGCGACATTTTTAT
GATGCGCTACAGGGTGCGCGCACGGCGTTTATTCTGGAGTGCAAGAAAGCGTCGCCGTCA
AAAGGCGTGATCCGTGATGATTTCGATCCAGCACGCATTGCCGCCATTTATAAACATTAC
GCTTCGGCAATTTCGGTGCTGACTGATGAGAAATATTTTCAGGGGAGCTTTAATTTCCTC
CCCATCGTCAGCCAAATCGCCCCGCAGCCGATTTTATGTAAAGACTTCATTATCGACCCT
TACCAGATCTATCTGGCGCGCTATTACCAGGCCGATGCCTGCTTATTAATGCTTTCAGTA
CTGGATGACGACCAATATCGCCAGCTTGCCGCCGTCGCTCACAGTCTGGAGATGGGGGTG
CTGACCGAAGTCAGTAATGAAGAGGAACAGGAGCGCGCCATTGCATTGGGAGCAAAGGTC
GTTGGCATCAACAACCGCGATCTGCGTGATTTGTCGATTGATCTCAACCGTACCCGCGAG
CTTGCGCCGAAACTGGGGCACAACGTGACGGTAATCAGCGAATCCGGCATCAATACTTAC
GCTCAGGTGCGCGAGTTAAGCCACTTCGCTAACGGTTTTCTGATTGGTTCGGCGTTGATG
GCCCATGACGATTTGCACGCCGCCGTGCGCCGGGTGTTGCTGGGTGAGAATAAAGTATGT
GGCCTGACGCGTGGGCAAGATGCTAAAGCAGCTTATGACGCGGGCGCGATTTACGGTGGG
TTGATTTTTGTTGCGACATCACCGCGTTGCGTCAACGTTGAACAGGCGCAGGAAGTGATG
GCTGCGGCACCGTTGCAGTATGTTGGCGTGTTCCGCAATCACGATATTGCCGATGTGGTG
GACAAAGCTAAGGTGTTATCGCTGGCGGCAGTGCAACTGCATGGTAATGAAGAACAGCTG
TATATCGATACGCTGCGTGAAGCTCTGCCAGCACATGTTGCCATCTGGAAAGCATTAAGC
GTCGGTGAAACCCTGCCCGCCCGCGAGTTTCAGCACGTTGATAAATATGTTTTAGACAAC
GGCCAGGGTGGAAGCGGGCAACGTTTTGACTGGTCACTATTAAATGGTCAATCGCTTGGC
AACGTTCTGCTGGCGGGGGGCTTAGGCGCAGATAACTGCGTGGAAGCGGCACAAACCGGC
TGCGCCGGACTTGATTTTAATTCTGCTGTAGAGTCGCAACCGGGCATCAAAGACGCACGT
CTTTTGGCCTCGGTTTTCCAGACGCTGCGCGCATATTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00909
UniProtKB Entry NameTRPC_ECOLI
GenBank Protein ID43192
GenBank Gene IDV00366
General References
  1. Christie GE, Platt T: Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions. J Mol Biol. 1980 Oct 5;142(4):519-30. [Article]
  2. Horowitz H, Van Arsdell J, Platt T: Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium. J Mol Biol. 1983 Oct 5;169(4):775-97. [Article]
  3. Yanofsky C, Platt T, Crawford IP, Nichols BP, Christie GE, Horowitz H, VanCleemput M, Wu AM: The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 1981 Dec 21;9(24):6647-68. [Article]
  4. Milkman R, Bridges MM: Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons. Genetics. 1993 Mar;133(3):455-68. [Article]
  5. 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 al.: 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. 1996 Dec 31;3(6):363-77. [Article]
  6. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  7. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  8. Krug K, Carpy A, Behrends G, Matic K, Soares NC, Macek B: Deep coverage of the Escherichia coli proteome enables the assessment of false discovery rates in simple proteogenomic experiments. Mol Cell Proteomics. 2013 Nov;12(11):3420-30. doi: 10.1074/mcp.M113.029165. Epub 2013 Aug 1. [Article]
  9. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  10. Wilmanns M, Priestle JP, Niermann T, Jansonius JN: Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution. J Mol Biol. 1992 Jan 20;223(2):477-507. [Article]
  11. Wilmanns M, Schlagenhauf E, Fol B, Jansonius JN: 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. 1990 Jan;3(3):173-80. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB035431-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-PhosphateexperimentalunknownDetails