Aminodeoxychorismate lyase
Details
- Name
- Aminodeoxychorismate lyase
- Kind
- protein
- Synonyms
- 4-amino-4-deoxychorismate lyase
- 4.1.3.38
- ADC lyase
- ADCL
- Gene Name
- pabC
- UniProtKB Entry
- P28305Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0017000|Aminodeoxychorismate lyase MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFW PQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEG ITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLF WRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMP VMPVCACGDVSFSSATLYEYLAPLCERPN
- Number of residues
- 269
- Molecular Weight
- 29714.78
- Theoretical pI
- 6.49
- GO Classification
- Functions4-amino-4-deoxychorismate lyase activity / pyridoxal phosphate bindingProcessesfolic acid biosynthetic process / tetrahydrofolate biosynthetic process
- General Function
- Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
- Specific Function
- 4-amino-4-deoxychorismate lyase activity
- Pfam Domain Function
- Aminotran_4 (PF01063)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0017001|Aminodeoxychorismate lyase (pabC) ATGTTCTTAATTAACGGTCATAAGCAGGAATCGCTGGCAGTAAGCGATCGGGCAACGCAG TTTGGTGATGGTTGTTTTACCACCGCCAGAGTTATCGACGGTAAAGTCAGTTTGTTATCG GCGCATATCCAGCGACTACAGGATGCTTGTCAGCGGTTGATGATTTCCTGTGACTTCTGG CCTCAGCTTGAACAAGAGATGAAAACGCTGGCAGCAGAACAGCAAAATGGTGTGCTGAAA GTCGTGATCAGTCGCGGTAGTGGCGGGCGAGGGTACAGCACATTGAACAGCGGACCGGCA ACGCGGATTCTCTCCGTTACGGCTTATCCTGCACATTACGACCGTTTGCGTAACGAGGGG ATTACGTTGGCGCTAAGCCCGGTGCGGCTGGGGCGCAATCCTCATCTTGCAGGTATTAAA CATCTCAATCGTCTTGAGCAAGTATTGATTCGCTCTCATCTTGAGCAGACAAACGCTGAT GAGGCGCTGGTCCTTGACAGCGAAGGGTGGGTTACGGAATGCTGTGCGGCTAATTTGTTC TGGCGGAAGGGCAACGTAGTTTATACGCCGCGACTGGATCAGGCAGGTGTTAACGGCATT ATGCGACAATTCTGTATCCGTTTGCTGGCACAATCCTCTTATCAGCTTGTCGAAGTGCAA GCCTCTCTGGAAGAGTCGTTGCAGGCAGATGAGATGGTTATTTGTAATGCGTTAATGCCA GTGATGCCCGTATGTGCCTGTGGCGATGTCTCCTTTTCGTCAGCAACGTTATATGAATAT TTAGCCCCACTTTGTGAGCGCCCGAATTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P28305 UniProtKB Entry Name PABC_ECOLI GenBank Gene ID M93135 PDB ID(s) 1ET0, 1I2K, 1I2L KEGG ID ecj:JW1082 NCBI Gene ID 946647 - General References
- Green JM, Merkel WK, Nichols BP: Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. J Bacteriol. 1992 Aug;174(16):5317-23. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- 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]
- 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]
- Green JM, Nichols BP: p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC. J Biol Chem. 1991 Jul 15;266(20):12971-5. [Article]
- Ye QZ, Liu J, Walsh CT: p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9391-5. [Article]
- Nakai T, Mizutani H, Miyahara I, Hirotsu K, Takeda S, Jhee KH, Yoshimura T, Esaki N: Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli. J Biochem. 2000 Jul;128(1):29-38. [Article]
- Parsons JF, Jensen PY, Pachikara AS, Howard AJ, Eisenstein E, Ladner JE: Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes. Biochemistry. 2002 Feb 19;41(7):2198-208. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide experimental unknown target Details