N-(5'-phosphoribosyl)anthranilate isomerase
Details
- Name
- N-(5'-phosphoribosyl)anthranilate isomerase
- Kind
- protein
- Synonyms
- 5.3.1.24
- PRAI
- Gene Name
- trpF
- UniProtKB Entry
- Q56320Swiss-Prot
- Organism
- Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
- NCBI Taxonomy ID
- 243274
- Amino acid sequence
>lcl|BSEQ0011097|N-(5'-phosphoribosyl)anthranilate isomerase MVRVKICGITNLEDALFSVESGADAVGFVFYPKSKRYISPEDARRISVELPPFVFRVGVF VNEEPEKILDVASYVQLNAVQLHGEEPIELCRKIAERILVIKAVGVSNERDMERALNYRE FPILLDTKTPEYGGSGKTFDWSLILPYRDRFRYLVLSGGLNPENVRSAIDVVRPFAVDVS SGVEAFPGKKDHDSIKMFIKNAKGL
- Number of residues
- 205
- Molecular Weight
- 23040.34
- Theoretical pI
- 6.55
- GO Classification
- Functionsphosphoribosylanthranilate isomerase activityProcessestryptophan biosynthetic process
- General Function
- Not Available
- Specific Function
- phosphoribosylanthranilate isomerase activity
- Pfam Domain Function
- PRAI (PF00697)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011098|N-(5'-phosphoribosyl)anthranilate isomerase (trpF) ATGGTCAGAGTGAAAATCTGCGGGATAACGAACCTGGAAGATGCACTGTTTTCTGTGGAG AGTGGTGCTGACGCTGTGGGATTCGTTTTCTATCCTAAGAGCAAAAGGTACATCTCTCCT GAGGATGCCAGGAGGATTTCTGTTGAATTACCTCCTTTCGTTTTTCGTGTGGGGGTCTTT GTGAACGAAGAACCAGAAAAGATTCTGGATGTGGCCTCTTATGTTCAGCTGAACGCGGTC CAGCTACATGGAGAAGAACCGATCGAACTGTGCAGAAAAATAGCGGAGAGAATCCTGGTG ATAAAAGCAGTTGGAGTTTCGAACGAAAGGGATATGGAACGTGCTTTGAATTACAGGGAA TTTCCGATTCTTCTCGATACGAAGACACCGGAGTATGGAGGAAGCGGAAAAACGTTCGAC TGGTCTCTGATCCTCCCGTACAGGGACCGGTTCAGGTATCTCGTGCTATCGGGAGGTTTG AATCCTGAGAACGTCAGAAGTGCGATAGACGTGGTTAGACCTTTCGCGGTGGATGTGTCT TCCGGTGTTGAGGCCTTTCCGGGAAAGAAAGATCACGATTCAATAAAGATGTTCATTAAA AATGCAAAGGGGTTGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q56320 UniProtKB Entry Name TRPF_THEMA GenBank Protein ID 3980232 GenBank Gene ID X92729 PDB ID(s) 1DL3, 1LBM, 1NSJ KEGG ID tma:TM0139 NCBI Gene ID 896969 - General References
- Sterner R, Dahm A, Darimont B, Ivens A, Liebl W, Kirschner K: (Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima. EMBO J. 1995 Sep 15;14(18):4395-402. [Article]
- Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [Article]
- Hennig M, Sterner R, Kirschner K, Jansonius JN: Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. Biochemistry. 1997 May 20;36(20):6009-16. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate experimental unknown target Details