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
Functions
4-amino-4-deoxychorismate lyase activity / pyridoxal phosphate binding
Processes
folic 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
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
ResourceLink
UniProtKB IDP28305
UniProtKB Entry NamePABC_ECOLI
GenBank Gene IDM93135
PDB ID(s)1ET0, 1I2K, 1I2L
KEGG IDecj:JW1082
NCBI Gene ID946647
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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
DrugDrug groupPharmacological action?TypeActionsDetails
D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamideexperimentalunknowntargetDetails