Aminodeoxychorismate lyase (P28305)

Identification
Name:Aminodeoxychorismate lyase
Synonyms:
  • 4-amino-4-deoxychorismate lyase
  • ADC lyase
  • ADCL
Gene Name:pabC
Enzyme Class:
Biological Properties
General Function:Involved in 4-amino-4-deoxychorismate lyase activity
Specific Function:Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Amino-4-deoxychorismate ↔ 1.0p-Aminobenzoic acid + 1.0Hydrogen ion + 1.0Pyruvic acid
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.04-Amino-4-deoxychorismate ↔ 1.0p-Aminobenzoic acid + 1.0Pyruvic acid
ReactionCard
SMPDB Reactions:
1.04-amino-4-deoxychorismate+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.04-amino-4-deoxychorismate + 1.04-Amino-4-deoxychorismate → 1.0Pyruvic acid + 1.0Hydrogen ion + 1.0p-Aminobenzoic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Amino-4-deoxychorismate ↔ 1.0p-Aminobenzoic acid + 1.0Hydrogen ion + 1.0Pyruvic acid
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.04-Amino-4-deoxychorismate → 1.0p-Aminobenzoic acid + 1.0Pyruvic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200854-Amino-4-deoxychorismateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01392p-Aminobenzoic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
GO Classification:
Function
4-amino-4-deoxychorismate lyase activity
binding
carbon-carbon lyase activity
catalytic activity
cofactor binding
lyase activity
oxo-acid-lyase activity
pyridoxal phosphate binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
folic acid biosynthetic process
metabolic process
Gene Properties
Blattner:b1096
Gene OrientationClockwise
Centisome Percentage:24.84
Left Sequence End1152523
Right Sequence End1153332
Gene Sequence:
>810 bp
ATGACGAAGCATACTCTTGAGCAACTGGCGGCGGATTTACGCCGCGCCGCAGAGCAGGGC
GAAGCGATTGCACCGCTGCGCGATCTGATTGGTATCGATAACGCTGAAGCGGCTTACGCC
ATTCAGCACATAAATGTGCAACATGACGTTGCGCAGGGGCGTCGCGTGGTAGGGCGTAAA
GTGGGCCTGACACATCCGAAAGTGCAACAACAACTGGGCGTTGATCAACCGGATTTTGGG
ACGTTATTTGCCGACATGTGTTATGGCGATAACGAAATCATTCCTTTTTCCCGTGTTCTG
CAACCCCGCATTGAAGCGGAGATCGCACTGGTGTTGAACCGCGATTTGCCCGCAACCGAT
ATCACCTTCGACGAATTGTATAACGCCATTGAATGGGTACTTCCGGCGCTGGAAGTGGTG
GGGAGCCGCATTCGCGACTGGTCGATTCAGTTTGTCGATACCGTGGCAGATAACGCCTCC
TGTGGGGTGTATGTCATCGGCGGTCCGGCGCAACGTCCGGCGGGGTTAGACCTGAAAAAC
TGCGCCATGAAGATGACGCGTAATAACGAAGAGGTTTCTAGCGGGCGCGGCAGCGAATGC
CTGGGACATCCGCTTAATGCGGCCGTCTGGCTGGCACGCAAAATGGCCAGTCTGGGTGAA
CCGCTGCGCACCGGAGATATCATTCTTACCGGGGCATTAGGTCCGATGGTGGCGGTGAAT
GCGGGCGATCGTTTTGAAGCCCATATTGAAGGCATAGGTTCAGTTGCTGCGACATTTTCA
AGCGCAGCCCCAAAAGGAAGTCTGTCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:269
Protein Molecular Weight:29715
Protein Theoretical pI:6
PDB File:1I2L
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aminodeoxychorismate lyase
MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFW
PQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEG
ITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLF
WRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMP
VMPVCACGDVSFSSATLYEYLAPLCERPN
References
External Links:
ResourceLink
Uniprot ID:P28305
Uniprot Name:PABC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674492
PDB ID:1I2L
Ecogene ID:EG11493
Ecocyc:EG11493
ColiBase:b1096
Kegg Gene:b1096
EchoBASE ID:EB1456
CCDB:PABC_ECOLI
BacMap:16129059
General Reference:
  • 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
  • Green, J. M., Merkel, W. K., Nichols, B. P. (1992). "Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme." J Bacteriol 174:5317-5323. Pubmed: 1644759
  • Green, J. M., Nichols, B. P. (1991). "p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC." J Biol Chem 266:12971-12975. Pubmed: 2071583
  • 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
  • Nakai, T., Mizutani, H., Miyahara, I., Hirotsu, K., Takeda, S., Jhee, K. H., Yoshimura, T., Esaki, N. (2000). "Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli." J Biochem 128:29-38. Pubmed: 10876155
  • 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
  • Ye, Q. Z., Liu, J., Walsh, C. T. (1990). "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 87:9391-9395. Pubmed: 2251281